Health Axis Blog Latest

Health-Axis Blog Latest


Our sister site Health Axis is a new blog set up to share information, articles, recommended sites, Pod cast reviews and more. Set up with myself here in the UK and Toney Pantalleresco over in Canada We aim to connect with as many people across the globe as possible to share information, news stories, tips tricks and remedies.



Health Axis News Round Up 29 December 2012




Physical Culture Main Page

                                                              Physical Culture

The first idea of a name for this site was to be called something like Modern Physical Culture. Some people might be confused by the term physical culture as it is not often used these days but once-upon-a-time physical culture represented health, strength and longevity. In the 1800’s and early 1900’s people would lift weights, eat whole foods, move around lots every day and they stayed lean, strong and robust well into their 80’s and even 90’s. Staying strong is paramount to good health especially as we age. The lack of exercise and movement in general amongst today’s society along with food that no longer resembles food, and a million man made chemicals in everything we eat drink or breathe, means that the baby boomers from the 1950’s and 60’s are now feeling the pace of life. Modern diseases is escalating beyond control and the health sector looks like it is about to collapse, we have the new generations being born in the US right now supposedly  to be the first generation not expected to out live their own parents, so it’s time to go back to basics.

Choose not to end up as a drug laced vegetable dependant on your family and society to look after you as you dribble your way through the last decade or two of your life on this earth. Remember simply eating real foods and participating in some kind of weight baring exercise is essential to living a full existence and avoiding disease, especially the kinds of diseases that are associated with old age. Many diseases seen as ‘the norm’ or common when we age are not actually ‘normal’ to getting old when you look at the very few tribal people and traditional living societies still around today.

Join the Physical Culture revolution today and live as long as you can as well as you can and enjoy every second you have on this planet

BodyBuilding Diets

Body Building Diets

Body-builders know how to get shredded. Still, there are many conflicting diets, and many a forum debate that rumbles on around the world, people arguing that one way works better than the other. One thing is for sure, for decades bodybuilders in the most part have been cutting carbs to get lean. (no I’m not carb bashing, its just a fact)

For Body-builders, diets are a little more extreme, They diet for a set period of time, 12 weeks 16 weeks or there abouts. Bodybuilders are looking to get down to….2% 3% or so with their body fat so this is not your average person looking for less love handles or even trying to see those elusive abs, even so, we can all learn from the bodybuilder / physique athlete. After all why not learn from the best? 

  Things need to be kept simple. And some no nonsense approaches like diets laid out by the following professionals are diets I like. They get results where results are needed. Remember though, every one is different and any of the following diets can be used to good effect but you should always look to personalise the diet when you know your body well.

  The Metabolic Diet 
Dr Mauro Di Pasquale has been writing books, personally helping people and handing out fantastic, science based information for years!

  Mauro is a man that has walked the walk and had a successful power lifting career. Just google the metabolic diet and see all the great reviews from people that have had success with it. The fact that it is still a popular book today shows you just how well this dieting  principle works.

Dave Palumbo    

Dave Palumbo was over 300lbs on stage at 1 or 2 % body fat when he competed as a Body-builder. Known for his column in a bodybuilding magazine writing as ‘The Anabolic Freak’ Dave is another man that has been there and do it all. Dave has worked with literally thousands of people getting ready for physique competitions and is a bit of a Nutritional Guru. If you can stick with his diet, you will achieve your dream physique.

Strong Lifts 5×5   

 Strong lifts 5×5 is a website dedicated to the basics. Lift heavy, lift consistently, eat whole foods and eat enough, And to be honest this works. Some times you can over think things. Many people, myself included spend too much time thinking of making the perfect routine and diet, and trying to incorporate the best of the rest to create our own unique program that’s going to produce the most amazing results ever! In reality, if we stick to the basics and stuck to them consistently we would improve dramatically.  Strong lifts is a basic. solid program that most people  can use and do well with.

Nutrition & Fat Loss

Nutrition is a huge topic and the more you learn the more you don’t know. Does that make sense? I don’t know. What I do know is that there will always be a debate as to the best diet. This is because of a few reasons that include factors such individual differences, environmental differences, lifestyle differences etc and that is not to mention the millions of pounds of pure profit that is made by keeping consumers guessing.  In this section I will provide my own ideas on nutrition along with articles from people in the industry that have proven results.

 I have included fat loss as part of this section because I believe nutrition to be the most important factor if fat loss. Although we should all be looking for the best nutrition to keep us healthy and disease free, most of us just want to loose some fat and look good

    Nutrition & FatLoss Information 


Fat Loss Tips Overview
A Quick Look At Diets
BodyBuilding Diets

Sunday 16th Jan 2011 – The Day Before…..

Well today is the day before. I am looking forward to starting tomorrow, I have had three  juices today and they really do make me feel good, placebo? possibly, or a sugar rush maybe? I made a shurbert lemonade with a whole small lemon and two apples and a while later i was feeling very good.   

  I went to the supermarket to by the stuff and every one was staring at my fully loaded green trolley! I was buying the list for two people as my girlfriend is also trying this severn day juice diet (although she has just told me that she has two lunch meetings this week but I have told her she’s only to have JUICE!) so i bought 70 apples, 5 cucumbers, 2 celerey, 12 lines, spinach, kale, parsley etc etc. 

 I know a bit about diet and nutrition and I am a bit of a weight lifter ( A very little bit recently) and I know the importance of Fats and Proteins so I have had to try very hard not to  modify this juice diet. I wanted to add the odd raw egg, scoop of whey or BCAA’s, some coconut oil, olive oil, walnut oil etc but i decided not to. It is only 7 days and  I want to give a good honest review about the whole  7lbs in 7 days diet and suggested exercise. 

 I Will no doubt experiment some more and improve on this program but for now,  i’m ready to start in the morning, jump on the scales and the juice my self to huge energy and mental clarity!! (apparently) 

10 New Year’s Resolutions for 2011

10 New Year’s Resolutions for 2011

Post a commentBy Ivan Wasserman, 23-Dec-2010

Related topics: Health claims, Regulation

2010 saw a flurry of enforcement activity by the Federal Trade Commission (FTC) based on claims made for dietary supplement and functional food products. There is no indication that 2011 will be any different.


Measure your claims carefully in 2011, unless facing an FTC complaint is one of your New Year’s Resolutions

Ivan Wasserman, a partner at Manatt Phelps & Phillips in Washington, DC, who specializes in the regulation of the marketing of such products, has identified ten New Year’s Resolutions to help keep your company from drawing regulators’ ire in 2011.

Resolution #1: I will not rely on “safety in numbers”

Just like you can’t get out of a speeding ticket for going 56 mph by arguing everyone else was going 80, the argument that ‘everyone else is doing it’ NEVER works at the FTC (or the FDA). There are a LOT of products and claims out there, and the regulators’ ‘speed traps’ cannot catch everyone.

Resolution #2: I will beware of “pixie dust”

As illustrated by the FTC’s recent settlement with NatureSmart LLC, if you highlight the fact that a product contains a particular ingredient, a regulator can consider it to be a claim that the ingredient is in the product at a significant level and, of course, has the claimed effect. Therefore, be sure that it is in the product at the amount needed to be effective.

Resolution #3: I will keep apprised of FTC/FDA enforcement actions and public comments

Especially in some of the ‘gray-er’ areas, knowing the opinions expressed by the agencies in the context of enforcement actions and in public comments will give you valuable information that you can use when deciding whether to launch a new product or tweak an existing one.

Resolution #4: I will stay away from miracle cancer cures for overweight children
As in the past, high on the agencies’ radars in 2011 are likely to be products that claim to treat serious diseases, products targeting children, and ‘miracle’ weight loss and similar products.

Resolution #5: I will have DBPCSS

Double Blind Placebo Controlled studies with Statistically Significant results are key to substantiating claims for dietary supplements and functional foods. While it is not a hard and fast rule, and there are certainly exceptions, if you find yourself in a position that you need to defend a claim that your product has an effect on health, anything less may leave you vulnerable.

Resolution #6: I will make sure my claims match my substantiation

Even with DBPCSS, you need to be sure that the claims match the study! Check the boxes: same product; same dosage; same target population; etc. And be careful not to overstate the results!

Resolution # 7: I will avoid claims that require FDA approval (unless I have it!)

As evidenced by the FTC’s settlements in cases like Iovate and Nestle, claims that require FDA approval and do not have it, i.e. claims that a product can treat, cure or prevent a disease, remain high on the FTC’s enforcement radar (and may violate FDA rules!). If challenged, it is likely to be very difficult to substantiate the claim to the FTC’s satisfaction.


Resolution #8: I will keep my customers happy

Perhaps most important, if your claims do not have the right support, your product may not have the right effect, and your customers will not be happy.

Resolution #9: I will be wary of being penny wise and pound foolish

The earlier a company involves qualified experts the better, as it can help prevent wasted dollars on inappropriate product development or promotion.

Resolution #10: I will have a successful 2011!

To end on a positive note, despite the need for caution, do not be scared to make great claims for great products. If you have a compliant claim with the right substantiation, by all means make it, and have a great 2011

Enzymes – The Forgotten Giver Of Life And Health



Without them there is no life. Lack of them can cause health problems, illness and death. In science we know allot  of information about enzymes yet ask anyone you know about them and they will have no idea what you are talking about. Yet  enzymes should be in our conscious and  on the menu constantly if we want to experience good health and longevity. Some people will have heard of digestive enzymes but not to many people use them. I am a massive fan of Serrapeptase for helping to relieve the pain and inflammation of GOUT! and for helping to “dissolve” scar tissue and  fibroids that  some women suffer with (also known as breast mice). We should all know more about Enzymes so Below is some information from my good friend Tony Pantalleresco’s web site. Have a read and Enjoy as they could save you from pain, discomfort and could even save your life!




  Skin Rash



  Mood Swings



  Hot Flashes


  Cold Hands and Feet  Neck and Shoulder Ache Sprue





 Back Weakness

 Fungal Forms


 High Blood Pressure


 Hearing Problems


 Gum Disorders



                          Chronic Allergies

                          Common colds


                          Irritable Bowel

                          Chronic Fatigue

                          Sinus Infection

                         Immune Depressed Conditions

    LIPASE DEFICIENCY                                                      

                           Aching Feet


                        Bladder Problems



                        Gall Bladder Stress


                        Hay Fever

                        Prostate Problems


                       Urinary Weakness



                       Heart Problems



Protease digests protein. Acidity is created through the digestion of protein. Therefore a protease deficiency results in an alkaline excess in the blood. This alkaline environment can cause anxiety and insomnia. In addition, since protein is required to calcium in the blood, a protease deficiency lays the foundation for arthritis, osteoporosis and other calcium-deficient diseases. Because protein is converted to glucose upon demand, inadequate protein digestion leads to hypoglycemia, resulting in moodiness, mood swings and irritability. Protease also has an ability to digest unwanted debris in the blood including certain bacteria and viruses. Therefore, protease deficient people are immune compromised, making them susceptible to bacterial, viral and yeast infections and a general decrease in immunity.



Amylase digests carbohydrates along with dead white blood cells (pus). When you are low in amylase you are a candidate for abscesses (inflamed areas with pus but not bacteria). Amylase is also involved in anti-flammatory reactions such as those caused by the release of histamine and similar substances. An Amylase deficiency can result in skin problems such as psoriasis, eczema, hives, insect bites, allergic bee and bug stings, atopic dermatitis, and all types of herpes. Asthma and emphysema may also be exacerbated by an amylase deficiency.



Since lipase digests fat and fat-soluble vitamins, lipase deficient people can be expected to have a tendency towards high cholesterol, high triglycerides, difficulty losing weight and diabetes. The future outcome of these tendencies is heart disease, which kills one out of two Americans. Lipase deficient people also have decreased cell permeability, meaning nutrients cannot get in and the waste cannot get out. The condition of vertigo or labrynthis, also called Meniere’s Disease (dizziness aggravated by movement such as walking or driving), can also result from lipase deficiency.



Cellulase breaks down the fiber in our diet. Because our body does not produce cellulase, this food enzyme is essential. We must eat it on a daily basis. Remember, ONLY RAW FOODS contain cellulase. Of all the enzymes, this deficiency carries with it the most categories of problems. The symptoms of cellulase deficiency can best be described as malabsorption syndrome (impaired absorption of nutrients, vitamins, or minerals from the diet by the lining of the small intestine). Malabsorption has many symptoms including lower abdominal gas, pain, bloating and problems associated with the jejunum and pancreas.



People who have malabsorption syndrome and cellulase deficiency also have a tendency towards sugar (sucrose, lactose, & maltose) and/or gluten intolerance. Sucrose, lactose and maltose are three common sugars which some people cannot tolerate. They are broken down and absorbed into the system by three enzymes; sucrase, lactase and maltase.



intolerant people cannot split the sucrose disaccharide into twin partners, two units of glucose. Glucose is a primary brain food so expect mental and emotional problems in people who cannot get glucose into the brain. Symptoms include depression, moodiness, panic attacks, manic and schizophrenic behavior and severe mood swings.



intolerant people also have classic symptoms which include abdominal cramps and diarrhea. Other allergic symptoms, including asthma, have been witnessed from the ingestion of lactose-containing products.



intolerant people are generally sensitive to environmental conditions. An intolerance to sucrose, lactose, or maltose may be worsened by a deficiency in sucrose, lactase, or maltase.



Enzyme Nutrition



by Ron Kennedy, M.D., Santa Rosa, CA

The energy of life is expressed through DNA, desoxyribonucleic acid. These magnificent, complex molecules reside in the genetic material located in the nucleus of each living cell. DNA contains both the program to create the body and the ability to mobilize the energy to carry out the job. The first order of creation by DNA in the daily process of living is the production of more DNA (when the cell divides), and the second order of creation by DNA is the production of RNA. RNA stands for ribonucleic acid and this molecule is made by DNA (and sometimes by other RNA) through DNA’s ability to copy amino acid sequences in a selective fashion. Whereas there is only one structure for DNA, there are many RNA structures depending on the job assignment of a particular molecule of RNA. While many molecules in the body can be considered essentially dead when measured alone, RNA inherits a full complement of the vital life force contained in DNA. The job of RNA is to make proteins (and other RNA). Proteins serve as building blocks of the body, as well as many other functions. A large percentage of lean muscle tissue, for example, is made of protein. Connective tissue, including fascia, tendon and bone also is made largely of protein.


A specialized type of protein is called an “enzyme.” Enzymes are protein molecules made by RNA and other enzymes with the ability to facilitate and speed up chemical reactions throughout the body. In the haphazard process, thought to have been the beginning of biochemistry in nature which eventually gave birth to life, amino acids formed and strung themselves together by chance into polypeptide chains some of which became enzymes quite by accident. These structures, which had the ability to speed up reactions between the molecules around them, made life possible. The reactions they facilitated otherwise took so long to happen as to put off the development of life to the infinite future. Enzymes are thought to have conspired with each other to create the first nucleic acids, very large structures which eventually evolved into RNA and DNA. There now are around 3000 known enzymes in the body and probably several thousand more as yet undiscovered, one for each kind of biochemical reaction which occurs there. Enzymes inherit from RNA a full measure of the vital life force originally given to RNA by DNA. Enzymes are both the parents and grandchildren of DNA, the source of our vital life force. In the context of the living body, enzymes are living molecular entities. Enzymes work by virtue of their shape. An enzyme molecule can be compared, in shape at least, to many short strings of pearls (amino acids) strung together. This long string folds in on itself as certain sequences of amino acids (pearls) are more attracted to each other than to other sequences, thus giving the enzymes a specific shape. At one point on the surface of this string of pearls, there exists something which looks like a keyhole. This is called the “active site” on the enzyme. When matched with its specific coenzyme (a vitamin, or mineral, or trace element) this “lock” has the exact inverse contour of the “key” which is contained in the molecule of the enzyme’s “substrate,” the molecule the enzyme wants to transform into a different molecule. When the substrate appears, it inserts the “key” into the “lock.” The molecular structure of the substrate is transformed into a different molecular structure, and both enzyme and the newly transformed molecule go on their merry ways. The slowest known enzyme (lysozyme) processes one substrate every two seconds. The fastest known enzyme (carbonic anhydrase) processes a phenomenal 36 million substrate molecules per minute. The shortest lived enzymes function for twenty minutes, and the longest are around and doing their jobs for several weeks. When an enzyme is worn out, it is broken down and disposed of by other enzymes, its component amino acids and polypeptide chains used to make new enzymes.

Dr. Edward Howell

Every area of knowledge in progressive medicine has its early champion, Broda Barnes in the study of hypothyroidism, Jens Moeller in the therapeutic uses of testosterone, for example. The study of enzymes is no exception. Dr. Edward Howell has clarified enzymes and enzyme therapy for us. We owe Dr. Howell a debt of gratitude for his pioneering work. In helping us understand the role of enzymes, Dr. Howell studied man, animals and plants with equal curiosity and scientific acumen. By comparative studies of disease states in man and in animals, Dr. Howell clearly demonstrated the disastrous nutritional effect of cooking food — more about that later.

            A Classification of Digestive Enzymes

Particular types of enzymes have digestive functions. The job of a digestive enzyme is to break down food during the digestive process. The intestine is more able to absorb food which is thus broken down into smaller units, and the rest of the body is more easily able to utilize food which is in this form. There are three basic types of digestive enzymes, one type for each class of food: lipase for fat, proteinase for protein and amylase for carbohydrate. Enzymes which drive the other processes of living are called “metabolic enzymes.” There is one enzyme for each type of biochemical reaction which happens in the body. Metabolic enzymes are by far the most numerous of all enzymes. Enzymes which are present in raw, uncooked food are called food enzymes to indicate where they come from: the food itself. They also are called “exogenous” enzymes, because they come from outside your body. Enzymes which are made in the body are called “endogenous” (meaning “inside-created”) and include both metabolic and digestive enzymes. Enzymes which are eaten with your food and are made by other animals or plants, are exogenous (outside-created). Food enzymes are exogenous enzymes. Exogenous enzymes have two origins: animal enzymes from animal food (raw meat, raw eggs, raw milk, etc.) and phytoenzymes, which come from plants (phyto = plant). Autolytic (meaning “self-digesting”) enzymes, which are very important in this discussion, are endogenous enzymes contained inside cells. The purpose of an autolytic enzyme is to break down the cell in which it is contained after that cell dies. Autolytic enzymes are contained in little bag-like structures which rupture upon death of the cell, releasing the autolytic enzymes to do their jobs. Because the body is made of fat, protein and carbohydrate, these enzymes are lipases, proteinases and amylase. It is important that you understand the above terminology for purposes of this discussion. I suggest you make a note card for each type of enzyme with a definition on the reverse side of the card. This terminology may seem confusing at first but as you study it, it begins to make an elegant kind of sense. The following flow chart will help you get all this straight.

Flow Chart of Enzymes

    I.   Endogenous Enzymes: (from inside the consumer or predator, i.e., you)

    A.  Human enzymes

    1.  Endogenous metabolic enzymes (made throughout the body)

                                                                          a.            Endogenous lipases

                                                                          b.            Endogenous proteinases

                                                                           c.            Endogenous amylase

     2.   Endogenous digestive enzymes (made only in the digestive tract)

     3.   Endogenous autolytic enzymes (also lipase, proteinase and amylase)

            Exogenous Enzymes:

      A.            Animal enzymes

    1.   Exogenous metabolic animal enzymes

     2. Exogenous autolytic animal enzymes

                                                                          a.            Exogenous animal lipases

                                                                          b.            Exogenous animal proteinases

                                                                           c.            Exogenous animal amylase

   B.  Phytoenzymes (of plant origin)

     1.   Exogenous metabolic plant enzymes

      2.  Exogenous autolytic plant enzymes

    a.  Exogenous plant lipases

  b.   Exogenous plant proteinases

 c.  Exogenous plant amylase

I have underlined the enzymes in which we have the most interest in this discussion. These enzymes can do a lot of work for us and save us a lot of energy. They are what this discussion is about.

     Enzyme Activators and Inhibitors

Enzymes in the activated state are very busy little guys. They must spend most of their lives inactivated, otherwise they would digest their host organism in a few minutes. The body has elaborate mechanisms to keep enzymes inactive until they are needed. The usual condition of an enzyme circulating throughout the body is that it is held in check by an amino acid chain, which is part of the enzyme — a kind of safety latch similar to the safety latch on a gun or the lock on a door. When the action of the enzyme is needed, an associated activating enzyme is released, for example, from an area of thrombosis (a clot — inside an important artery, let us say) or, to use another example, from an area of inflammation. This activating enzyme turns off the safety latch or, in the other analogy, unlocks the door, allowing the enzyme to go to work, causing a breakdown of the blood clot or cleaning up the inflammatory debris. Another safety system is that of enzyme inhibitors. These are proteins, which fit into the active site of the enzyme molecule, thus preventing the admission of substrate (the stuff the enzyme is designed to break down). When the enzyme is needed , these proteins are signaled to release themselves from the enzyme thus freeing the enzyme to do its assigned task. Examples of exogenous enzyme inhibitors include many antibiotics, which kill bacteria by inhibiting key enzyme systems. Unfortunately, they also inhibit the identical metabolic enzyme systems in the body and thus are toxic to both bacteria and host. (You are the host.) This is one more reason I prefer to avoid the use of antibiotics, if at all possible. Another example of exogenous enzyme inhibitors are those contained in seeds and nuts (which are also seeds). From seeds (nuts are seeds) entire plants grow with only the addition of water, soil, sunshine and the right temperature. From these facts, you can guess that seeds are loaded with enzymes. However, they must be held in the inactive state until water is present. Nature has loaded seeds with enzyme inhibitors, which are deactivated by the addition of water. This process is called “germination.” Therefore, when you chow down on your favorite seeds and/or nuts, you are loading your stomach with enzyme inhibitors. These enzyme inhibitors slow down or stop the action of whatever digestive enzymes may be present with your food, whether from an endogenous or exogenous source. Therefore, either avoid seeds and nuts unless (1) you germinate them first by letting them soak in water for a few days or (2) you consume them along with sufficient extra enzyme powder to neutralize the enzyme inhibitors.

    Misconceptions About Enzymes

Professor B. P. Babkin wrote, in 1935, that when the pancreas is stimulated to secrete enzymes for digestion, it secretes equal amounts of proteinase, lipase and amylase. This was known as the “Theory of Parallel Secretion of Enzymes.” (These three enzymes are responsible for digesting protein, fat and carbohydrate respectively.) Babkin’s theory held that if you ate a meal of almost all protein, for example, your pancreas would pour out enzymes to digest not only protein but also fat and carbohydrate as well, and that these latter two enzymes would simply go to waste. The Theory of Parallel Secretion implied that enzymes are so easy for the body to manufacture, it can afford the luxury to make some and then throw them away! Regardless of how little sense this made, the theory was accepted and taught in medical schools because of the reputation of the eminent Dr. Babkin. This is an example of the operation of dogma in medical thought. The eating and digestion of dogma in medical schools is identical to the same process in theology and law schools. No enzymes are required, only lame brains. It is now known that the pancreas exhibits “selective secretion,” meaning that the organ is signaled as to what sort of food is present and needing digestion, so it can then secrete the enzymes which are specifically needed for that kind of food. This is not only experimentally true, but it also makes sense! Given how complex and specific enzymes are, obviously a lot of energy is required to create them, and it makes no sense that the body would then waste them. No intelligent being would create such a mechanism in the human body, or any other body for that matter. Nevertheless, many doctors have not reconsidered what they were taught in medical school and find the idea of “enzyme therapy” to be absurd because, as they think they know: enzymes are so easy to make, the body is willing to waste them and, being so insignificant, they could not possibly constitute a valuable therapy. For many years it was taught in medical school biochemistry classes that an enzyme was not changed in any way when it performed its function of facilitating and speeding up a reaction. Enzymes were thought to act as true “catalysts,” just as some metal ions do in purely non-biochemical chemical reactions. This is now known not to be the case. Enzymes are used up and destroyed in the process of doing their jobs, and the remains must be disposed. They are broken down by other enzymes and new enzymes are made to replace them. Enzymes do last a long time: from twenty minutes to a few weeks, doing the same job many times before wearing out. Enzyme creation and destruction is happening throughout the body at all times. It only stops when the organism dies and actually not even then as we will now see. It was also once taught in medical schools that enzymes could not pass through the gut wall and, therefore, any exogenous enzyme would have to first be digested, i.e., broken down to its component amino acids like any other protein, before it could be absorbed and used by the body. It is now known that both enzymes and ordinary proteins can be absorbed whole without being fully digested. The fact of antibody (which is protein) absorption directly through the gut wall is the basis for the transmission of immunity from mother to child through breast feeding. This has enormous therapeutic implications where enzymes are concerned, because once in the body an exogenous enzyme identical in structure to an endogenous enzyme can be used as though it were an endogenous enzyme — the body has no way to distinguish it from an enzyme made inside the body.

   Comment on Medical Politics and Dogma

The medical dogma that proteins could not be absorbed without being broken down to the component amino acids died hard in standardized medical circles and medical schools, and this delayed the popular perception of the value of oral enzyme therapy immeasurably. The heyday of enzyme therapy has not yet come in the United States, although it certainly has arrive in other countries, notably Europe and Japan. It is truly unfortunate that the medical establishment in the U.S. is so intensely nationalistic as to believe that if a therapy has not been proven inside the boundaries of the U.S.A., then it is worthless until proven otherwise.


All animals and plants contain the enzymes to “autolyze” themselves when they die. “Autolysis” literally means “self breaking” and refers to the fact that plant and animal tissues digest themselves after they die. Nature, folks, has thought of everything. The Egyptians developed a process to prevent bacterial breakdown of the body after death; however, they could not solve the problem of enzymatic autolysis. Therefore, a mummy, while it retains the essential form of the original body, is not exactly ready for a hot date. This fact, autolysis, leads us into the field of enzyme therapy. Unfortunately for humans, we have discovered how to cook our food. Cooking destroys the autolytic enzymes contained in food! All enzymes are extremely heat sensitive. If you cook them, they die! While pre-fire man received all the benefits of exogenous enzymes, post-fire man is starved for exogenous enzymes and must rely almost entirely on endogenous digestive enzymes, those he makes for himself.

       The Function of Fever

If you raise temperature a few degrees above normal body temperature, enzymes become hyperactive. The enzymes in the immune system are activated and powered up to fight infection by acceleration of the activity of certain white cells which literally eat and digest bacteria. This process is called “phagocytosis,” which means literally “eating cells.” At 104 degrees Fahrenheit, enzymes and phagocytic cells are at their maximum state of activation. Therefore, a fever should not be artificially brought down unless it exceeds 104 degrees Fahrenheit. At 106 degrees, brain damage (i.e., enzyme destruction) begins. When there is a fever it should be monitored every thirty minutes and treated if it exceeds 104.

    Cooking: The Great Nutritional Disaster

If you raise the temperature to 118 degrees for a few minutes enzymes are completely destroyed. It is practically impossible for the body to create such an intense fever; however, cooking can easily exceed this temperature. Therefore, cooking, even at low temperatures, is the death of enzymes.Since man mastered the use of fire, the practice of cooking food has been with us. From a nutritional standpoint, this was a great disaster. Let me explain that. Enzyme production is so labor-intensive that the eating habits of animals in nature are designed to take advantage of the presence of living enzymes in food. Fortunately for animals, they have not discovered how to cook their food.

      The Overgrown Pancreas

Because of cooking, our digestive organs, especially the pancreas, are called upon to do the job of enzyme production alone. In a person who eats even a moderate percentage of cooked food, the pancreas is hypertrophied (overgrown) to two or three times its normal size (that size found in people who eat only raw food).Animals in the wild eat raw food and their pancreases are approximately 1/3 the size of the typical human pancreas when corrected for body weight. Those animals are busy taking advantage of exogenous digestive enzymes contained in the raw food they eat. 

“So what?” you ask. So what, is that you have an organ (the pancreas) which is hypertrophied and is begging, borrowing and stealing from the rest of the body, so that enough enzymes can be produced to digest the food you eat. The precursors of metabolic enzymes, the amino acids and polypeptides, which are needed in the rest of the body are being hogged up by the pancreas to produce digestive enzymes because the pancreas is getting no help from the enzymes contained in raw food. Cooking has destroyed them. It is this simple: if living enzymes can be derived from food sources, the body does not have to expend its precious energy making digestive enzymes in large quantity. It can utilize that energy in the process of living healthier and longer by concentrating its ability to make enzymes on the production of metabolic enzymes. This is important. If you do not understand this, read it again until you do.

    Cooking Milk

Pasteurization — the heating of milk to 145 degrees centigrade for thirty minutes — totally destroys not only bacteria from sick cows but all enzymes as well. There was a time, before the turn of the nineteenth into the twentieth century, when doctors recommended a raw milk diet for the cure of many diseases. This was before cows were locked up, pumped up (on drugs and enzymeless feed) and sucked out, but rather were allowed to roam freely, foraging for raw plant food and came in every morning to be milked by hand. Unpasteurized and unhomogenized milk, made in this fashion, is loaded with valuable enzymes and, if you can find it, will serve as a therapy for a number of diseases. Given what has happened to milk in this century, informed doctors recommend that you avoid milk like the plague rather than drink it as a treatment for illness. It was inevitable, I guess, that man would finally think of cooking (pasteurizing) milk also. This avoids the necessity to monitor the milk cows to insure that they are free of disease.

     Eat Raw Meat? Thanks, But No Thanks

While it is true that raw meat contains loads of living enzymes, I am not suggesting that you eat raw meat. Given how animals are treated in modern animal husbandry, you cannot count on raw meat for being only raw meat. It also will contain hormones, antibiotics, herbicides and pesticides before and after cooking. Also, there is the matter of how it tastes.

        But The Eskimos Did!

For primitive, fireless man and for Eskimos, before acculturating to white man ways, raw meat was a great source of energy which kept these people free from degenerative diseases. The name “Eskimo” is an Indian term meaning “he eats it raw.” Alas, it is no longer so. Most Eskimos now are eating potato chips and hamburgers, having adopted the white man’s habits. Eskimo forebears knew empirically (simply by observation) that raw food, even raw meat, is healthy food. Nature has designed a process of assisted autolysis using both cathepsin made in your stomach and cathepsin contained in the raw meat. Cathepsin is a proteinase enzyme, able to break down protein, including meat. Eskimos did not know this explanation, but they knew they felt good and stayed healthy when they ate raw meat. Besides, that was almost all that was available to them. Vegetables do not grow so well in snow and ice. The only choice the Eskimos had was to cook their meat or not. Empirically, by the way they felt after eating raw meat, they chose not to cook it.The problem with raw meat is, of course, the possibility of infection with parasites living in the meat. However, in the colder climates meat-borne parasites are non-considerations. Because the life cycles of most parasites involve an out of body experience (out of the body of the host, that is), usually at the egg or larval stage, they are not able to survive in cold weather — they bite the ice, usually by having their eggs or larvae frozen solid. They do thrive, on the other hand, in warm tropical climes, and they do well in temperate climes. Eskimos did not have the parasite problem. The point of this discussion about Eskimos is that the phobia of meat and fat is not justified. We should focus our attention where it belongs: the fact that cooking is the real culprit. If you are a vegetarian and you cook your vegetables, guess what? You would be better off not doing that.

     Stomach Physiology

The first part of the stomach, called the “antrum” or “cardia,” or as Dr. Howell named it: the “food enzyme stomach,” is similar in function to the “extra” stomach(s) in ruminants (cattle, deer, elk, moose, etc), in cetacea (whales, porpoises and dolphins) and in seed-eating birds such as chickens and pigeons. In all of these animals, the first stomach (or stomachs in some cases) and the food enzyme stomach in man, are where, together with cathepsin contained in raw meat, protein is partially digested. Of course, if you cook the meat, that portion of exogenous cathepsin is destroyed. In the food enzyme stomach, fats and carbohydrates eaten from raw sources (and thus containing lipases and amylase for autolysis), proceed to autolyze (predigest) themselves. In the food enzyme stomach, food is allowed to autolyze as much as it will for a period up to one hour. In humans, the food enzyme stomach functions as a separate organ by virtue of the fact that the lower stomach, also called the “fundus” or “pyloric stomach” (it could also be called the “endogenous enzyme stomach”), remains shut, the potential space closed by forcible opposition of the anterior and posterior walls of the stomach against each other. After autolysis the fundus opens, receiving the food, making a load of hydrochloric acid and pepsin and proceeding with digestion. Under “normal” circumstances of raw sources of protein, about half the stomach digestion of protein is achieved in the antrum or food enzyme stomach with cathepsin and other autolytic enzymes and the other half in the fundus with pepsin and hydrochloric acid. The typical doctor might disagree with this description and cite “barium swallow” fluoroscopy studies which show the entire stomach frantically contracting and relaxing after a barium swallow. This may be how the stomach behaves when insulted with a solution of barium, but barium is not food! The stomach behaves differently when engaged in digestion and is not being assaulted by a barium swallow. If your stomach contracted frantically after a meal you would know it, you would not need a barium assault to prove it. The point is: we can see by the behavior of the stomach during digestion that it is designed to take advantage of the enzymes which are contained in raw foods, so that we do not have to expend the large amounts of energy and resources necessary to make a huge load of endogenous digestive enzymes to do it on our own.

      Exogenous Enzymes and Longevity

Lest you still are not taking this discussion seriously, let us consider some research relating to enzymes, health and longevity. Because insects are cold-blooded and short-lived, it is easy to demonstrate the value of enzymes to their longevity. A study done with Daphnia magna, the water flea, demonstrated that raising its environmental temperature from 46 degrees to 82 degrees Fahrenheit cuts its life-span to 1/4 of that at 46 degrees. Increased temperature raises enzyme activity, and when enzyme vitality is used up, life is over. The same can be said for you, not because of increased temperature — because you are a warm-blooded animal, able to regulate your temperature — but because you deplete your enzyme stores in another way: by eating cooked food and requiring your body to divert precious resources to making digestive enzymes. This shortens your life span and robs you of your natural state of health. Many people, even people otherwise well-educated in nutrition, do not take the idea of enzyme support seriously. Many seem to think that enzyme support should be done only if the pancreas is weak, while the truth is that it should also be done if it is strong. If the pancreas is strong — enlarged and producing triple doses of enzymes, thus robbing the rest of the body, including the immune system, of precious enzyme precursors — we would do well to supplement endogenous enzyme production with exogenous food enzymes contained in raw foods. People who eat lots of raw food live longer and feel better. If you are interested in living long and remaining healthy, perhaps I can get your attention with the fact that enzyme production, both digestive and metabolic, decreases with age. When the enzymes finally check out, so do you. Maybe Methuselah really did live a long time, if he ate pure raw food as the Bible assures us that he did. However, if he lived in excess of 900 years, we still need to know more about how he did that! Most scientists consider this account fiction; however, I prefer to keep an open mind about things outside my personal experience.

         Enzymes and Obesity

Still don’t have your attention? Let us talk about being fat. Have you noticed how many people are overweight, I mean, uh, fat? You may be one of them. If the body is starved for the vital energy of enzymes which have been depleted in the cause of digestion, that body craves more energy. The only way the body knows to get more energy is to eat, and the only way to insure that you eat is to create the experience of hunger. So you eat and eat and eat, trying to get satisfied. What is missing is not calories but vital life energy, which has been robbed from your enzyme system. So you eat more dead, enzyme-free food, the calories are stored as fat, and the craving goes on. You can eat more calories and lose weight, if your source of calories is raw food because you are consuming vital life energy, i.e., enzymes, with your food, and this energy will convert more food to motion and thought and less to fat. When the body is presented with exogenous food-derived enzymes, it is able to make more endogenous enzymes for metabolism. One class of endogenous enzymes is lipase. The job of lipase is to break down fat. Got a fat problem? Get some lipase. Lipases are contained in all raw, uncooked food containing fat. Do not be afraid of fat, be afraid of fatty food which has been cooked and stripped of its autolytic lipases. Remember what Einstein taught us: mass and energy are interchangeable. With exogenous, food-derived enzymes, you can convert some of your mass to energy, maybe not at the speed of light squared, but fast enough.

           Too Skinny?

Some people weigh much less than they want to weigh because their pancreas has been exhausted by a lifetime of no support from exogenous enzymes. This person may eat loads of food and yet remain underweight. The solution for such an underweight individual is not to eat more but to digest better. If pancreatic exhaustion is the problem, digestive enzyme supplementation is the solution and will produce better digestion and dramatic weight gain.

      Fasting and Enzymes

It has long been known by practitioners of fasting that health can be restored by this ancient practice. Water fasting — no food consumed, only pure water — relieves the body of the necessity of producing enzymes for digestion. The enzyme precursors can therefore be used for metabolic enzyme production. The same is true in juice fasting, which requires that only freshly prepared vegetable juices, and sometimes a smaller quantity of freshly prepared fruit juices, be consumed along with pure water. In this kind of fasting, fresh enzymes are given to the body in concentrated form in the juice. If illness is present, it may be helped through fasting. The immune system is given what it needs to correct illness — enzymes — and thus a sufficient supply of enzyme precursors. There may be a “healing crisis,” or detoxification stage, which is uncomfortable to go through but which leads to a new level of vital health. Fasting can be considered a form of enzyme therapy.

      Enzymatic Therapy For Arthritis

Still not convinced? Lets talk about treating and avoiding disease. In the 1940s, Dr. Arnold Renshaw of Manchester, England suspected rheumatoid arthritis to be a digestive disease. He based his suspicions, published in the Annals of Rheumatic Disease in 1947, on many observations at autopsy of the small intestines of people who had rheumatoid arthritis at the time of death. He found the small intestines to be consistently atrophied. Dr. Renshaw tested his hypothesis by having an enzyme preparation made for oral administration. He found that rheumatoid arthritis patients improved dramatically in just over one half of 556 patients. Another 219 of these 556 patients were improved to a lesser extent.He also discovered that the pain of osteoarthritis could be helped with enzyme therapy. The time required for improvement in these illnesses varied from two months to two years, so persistence is the key in this type of therapy. Similar results can be obtained with raw diets. It may be a long time to wait for results, but for most people it is worth waiting for and easier to confront knowing that this type of therapy benefits the rest of the body as well.

         Enzyme Therapy For Cancer

You may have heard of cases of cancer cured using only raw foods. If this happens, one of the explanations is clear: the immune system is powered up by a surge of enzyme precursors available when exogenous food enzymes are added to the diet, thus allowing the immune system to defeat (eat? digest?) the cancer. Enzyme treatment is the most exciting and promising approach to cancer. It attempts to duplicate the spontaneous cancer cures which are sometimes seen in oncology. Some doctors, including Dr. Howell, offer enzyme therapy for treatment of cancer. It stands to reason that if a prolonged fast or a diet of only raw vegetables can help some cases of cancer, massive doses of enzymes should also be able to help. This kind of therapy is done in a hospital and involves frequent small meals and doses of enzymes every thirty minutes. The need for careful supervision is obvious. I do not offer such a therapy, however, the folks at the Bradford Research Institute in Tijuana, Mexico offer this therapy along with others.

        Enzymes and Allergy

It is undeniable that some people react to certain foods. The explanation is that digestion is proceeding badly due to poor enzyme and/or stomach acid production. This causes food to arrive in the lower small intestine and colon relatively undigested. This upsets the normal flora of bacteria found there by favoring those bacteria able to digest that food. These bacteria replace so-called friendly species of bacteria which normally live symbiotically with us. The overall result is a condition called “dysbiosis” and malabsorption. The body forms antibodies to foods and bacterial breakdown products in the lower gut. These antibodies also attack, as if to neutralize, normal tissue of the body such as joint and skin tissue. Arthritis and skin disease are only two examples of diseases which have their origin in disordered digestion, diseases which have long been considered incurable in medical circles.

         Lipase and Atherosclerosis

As we grow older, the supply of all endogenous enzymes decreases. This includes lipase. It may be that the decrease in lipase as a function of aging has a lot to do with fatty deposits on the walls of arteries and the acceleration of atherosclerosis. Decreased supplies of lipase occurs in the intestines and in the serum (the noncellular part of blood). Therefore, as we grow older, it becomes increasingly important to either cut fat intake or to ingest exogenous lipase along with fat to help prevent atherosclerosis. This means raw food or supplementation with enzyme powder. Elsewhere, I have expressed the opinion that fat is not so disagreeable to the human body (provided there are plenty of antioxidants on board), rather what is in the fat constitutes the problem: herbicides, pesticides, synthetic hormones, antibiotics, etc., all fed to cattle to increase production. For an older person, it also may be that it is what is not in the fat: lipase is not in the fat if the fat is heated to 118 degrees Fahrenheit for only a few minutes. A rational approach to vascular disease is to load up on lipase with each meal containing fat. If you cannot bear to eat raw meat and you have no access to raw dairy products, buy some enzyme powder from your friendly health food store or organic grocery. In this manner, you can obtain the nutrition contained in the fat (the most powerful source of calories available) and not have to be concerned with the consequences. Nevertheless, it is not wise to unbalance your food intake in any direction, including excess fat.

           Comparative Pathology

Let us see how can we be relatively sure of the importance of ingesting exogenous enzymes. Domesticated animals suffer the same degenerative diseases which humans are subject to: cancer, arthritis, atherosclerosis; whereas this does not happen with animals in the wild. Animals procured from the jungle, when dissected, show no evidence of arthritis, cancer, or atherosclerosis, unless they live close to human pollution. But pity the health of the animal in captivity which is fed processed food. The explanation which makes the most sense to me is that domesticated animals fed processed food, because they receive no exogenous enzymes, fall ill with the same diseases we have. Processed human food (heat is part of the “process”) is stripped of its enzyme content. It is what some people call “dead food.” The animal equivalent is dog and cat chow, as well as cattle and chicken feed, which has gone through heat processing. This stuff is the animal version of the dead food we eat ourselves. Animals in the wild must eat fresh raw food, because nothing else is available. Therefore, they receive liberal amounts of all enzymes.

    The Point

The purpose of this discussion is to point out to you the importance of enzymes. Enzymes are not yet in the consciousness of the public, whereas the importance of vitamins and minerals is firmly entrenched. Your nutritional regime is not complete until cooked-food-induced enzyme starvation is corrected.  The best solution, of course, would be to revert to raw food exclusively. The next best solution would be to revert to eighty percent raw food. A salad with your meal is a nice gesture, but it is not enough, although every little bit helps, I suppose.If you are not able or, more likely, not willing to make the change to exclusively raw food, the next best solution is to supplement your diet with enzymes. These should be taken just as you begin to eat, and they should be in powder form. If you have the type which is powder in a capsule, separate the capsule, and pour the powder on your first bite of cooked food after it has cooled to around body temperature (otherwise, the enzyme is destroyed by the heat of the food). Do not use the tablet form of enzymes unless you chew it up.


§                              Ambrus JL et al. Absorption of exogenous and endogenous proteolytic enzymes Clin. Pharmacol. Ther. 8:362;1967.

§                              Barrett AJ Proteinases in mammalian cells and tissues Elsevier, North Holland Biomedical Press; 1967.

§                              Baumueller M XXIV FMS World congress of sport medicine Symposium on enzyme therapy in sports injuries May 29, 1990, p. 9 Elsevier Science Publishers, Amsterdam 1990.

§                              Beard J Enzyme therapy of cancer. In: Wolf, M. (Hrsg.) Maudrich-Verlag, Vienna;1971.

§                              Blonstein JL Oral enzyme tablets in the treatment of boxing injuries Practitioner 198: 547; 1967.

§                              Bramwell FWR The transmission of passive immunity from mother to young Frontiers of Biology, Vol. 18, North-Holland, Amsterdam;1970.

§                              Ekerot LK, Ohlsson K, Necking L Elimination of protease-inhibitor complexes from the arthritic joint Int. J.Tissue Reac. VII:391;1985.

§                              Emele JF, Shanaman J, Winbury MM The analgesic-anti-inflammatory activity of papain Arch Int Pharmacyn Ther 159:126;1966.

§                              Gardner MLG Intestinal assimilation of intact peptides and proteins from diet — a neglected field? Biol Rev 59:289-331;1984.

§                              Jaeger H Hydrolytic enzymes in the treatment of HIV disease General Medicine (Allgemeinmedizin) 19(4):160-164;1990.

§                              Layer P, et. al Fate of pancreatic intestinal enzymes during small intestinal aboral transit in humans Am J Physiol Gastrointest Liver Physiol 251:475;1986.

§                              Lopez DA, Williams RM, Miehlke M Enzymes, The Fountain of Life The Neville Press Inc. 1994 ISBN 1-884303-00-5.

§                              Neuhofer C Enzyme therapy in multiple sclerosis Hufeland Journal 2:47-50;1986.

Howell E Enzyme Nutrition, The Food Enzyme Concept Avery Publishing Group Inc., Wayne, New Jersey 1985 ISBN 0-89529-221-1.



“How is it possible that I am sick even though I eat the most organic foods, am very careful with my diet and exercise regularly?”

The answer tends to be: ENZYME DEFICIENCY.

The following is a brief summary of several of the more common enzyme deficiency conditions.

~~~: Protease digests protein. What happens when you are protease deficient? You will have protein deficiency symptoms, depending on how deficient you are in protease. Protease deficiency creates alkaline excess in the blood. This is not because protease itself is acidic; it is not. Acidity is created through the digestion of protein with protease. Some people may be vegetarian not by choice, but because they are protease deficient and cannot digest protein. Since acidity comes from the digestion of protein with protease, protease-deficient people may have an alkaline excess which can produce anxiety states. Often people take tranquilizers such as Xanex and then they zombie around in a fog, when simply taking protease can, through increased digestion of protein, acidify them to HOMEOSTASIS with resulting relief of their anxiety. Homeostasis is the dynamic equilibrium within the body. Without successful physiological homeostasis (balance), in which relatively constant conditions are maintained in the internal environment, the body cannot survive. The maintenance of homeostasis involves a number of factors in addition to metabolism, such as water intake and retention, acid-base balance, excretion of waste matter and control of body temperature. In other words our body will do whatever it must to stay in homeostasis. Protein is also required to carry protein-bound calcium in the blood. Insufficient protein-bound calcium lays the foundation for arthritis and other calcium deficient diseases. Why? When the blood cannot carry calcium because it lacks protein, it withdraws the necessary calcium from the bones to maintain homeostasis. This situation is aggravated in people who take calcium carbonate supplements, such as Tums or other antacids, because this adds to the alkaline stress on the blood. The blood cannot carry ionic calcium as efficiently because ionic calcium requires a certain level of acidity to be present. Overly alkaline people have a multitude of calcium metabolism problems, such as osteoarthritis, osteoporosis, gouty arthritis, degenerative disc problems, bone spurs and related disorders such as sciatica and ligament problems. Because 46% of digested protein is converted to glucose upon demand, inadequate protein digestion leads to hypoglycemia (hypoglycemia also has other causes such as hypothyroidism and vitamin deficiency). Symptoms include moodiness, mood swings and irritability among many others. Water follows protein (literally). Inadequate protein in the blood also means inadequate water. Where does the water go? Into the tissues after the protein! This causes tissue swelling (edema ). Water is forced into the capillaries and into the tissues by the pressure of blood being pumped around the body. By a reverse process, which depends on the water-drawing power of the proteins in the blood, it is reabsorbed in the capillaries from the tissues. These two mechanisms need to remain in balance. Protein maldigestion leads to a toxic colon. People in this category often have problems in the area of the descending colon (lower right quadrant of the abdomen). This includes developing appendicitis and even more serious problems such as mucous colitis and even colon cancer. Another of the most common results of protein maldigestion is chronic ear infections and fluid in the ears, especially in children. This is a protease calcium deficiency. To drain fluids from the middle ear, you must increase protease in the blood. Protease will pull water out of the middle ear, and also the ankles, hands and feet during PMS, and put it back into the blood. Protease is also involved in the immune system via its action on bacterial debris, certain viruses, and its ability to break down circulating immune complexes. Protease has an ability to digest unwanted debris in the blood and should be considered your friendly blood cleanser. Protease deficient people are immune compromised, making them susceptible to bacterial, viral and yeast Infections and a general decrease in immunity. Protease deficient women are predisposed towards PMS. The only people who cannot tolerate protease are those who suffer from ulcers, gastritis or hiatus hernias. The already damaged mucosal tissue cannot handle the extra acidity from the digested protein


~~~AMYLASE DEFICIENCY CONDITIONS: Amylase digests carbohydrates or polysaccharides into smaller disaccharide units, eventually converting them into monosaccharides such as glucose. People who are fat intolerant (can’t digest fats) often eat sugar and carbohydrates to make up for the lack of fat in their diet. If their diet is excessive in carbohydrates, they develop an amylase deficiency and symptoms arising therefrom. Amylase digests not only carbohydrates but also dead white blood cells (pus). For example, when you are low in amylase you are a candidate for abscesses (areas with pus but not bacteria). if you have a toothache and are being treated with antibiotics, but it doesn’t go away, chances are you may have an abscess. Amylase is involved in anti-inflammatory reactions such as those caused by the release of histamine and similar substances. The inflammatory response usually occurs in organs which are in contact with the outside world such as the lungs and skin. These include skin problems such as psoriasis, eczema, hives, insect bites, allergic bee and bug stings. atopic dermatitis, and all types of herpes. The lung problems including asthma and emphysema require amylase plus other enzyme formulas depending on the particular condition. Carbohydrates require phosphorus. If excess refined carbohydrates are consumed, a phosphorus deficiency will result.  ~~~Phosphorus deficiencies include: thick blood, tendency towards gastritis (inflammation of the gastrointestinal tract) and stiff joints, especially in the morning. Why stiff joints? Adequate phosphorus prevents the deposit of calcium oxalate and calcium carbonate in the joints. If phosphorus is deficient due to excess consumption of sugar, joint pain results from deposits of oxalates and carbonates Phosphorus deficiency is often accompanied by thick blood and high blood pressure. Please do not feel you can run out and get a phosphorus supplement to solve this problem. Quite the contrary. The only way the calcium and phosphorus can be balanced is by getting them both from the foods in which they originate in a natural, balanced proportion.

~~~LIPASE DEFICIENCY CONDITIONS: Since lipase digests fat and fat-soluble vitamins, lipase deficient people can be expected to have a tendency towards high cholesterol, high triglycerides, difficulty losing weight and diabetes or a tendency towards glucosuria (sugar in the urine without symptoms of diabetes). The down-the-road outcome of these tendencies is heart disease. Because lipase requires the co-enzyme chloride, lipase deficient people have a tendency towards hyphochlorhydria (low chlorides in our electrolyte balance). This can be easily remedied with lipase, but often nutritionists recommend using betaine HCL, which places acidic stress on the blood, leading to an inability to provide the alkalinity required to activate the body’s pancreatic enzymes. Lipase requires a high pH for its activation among food enzymes. That is why fats are the hardest of all foods to digest. Fat intolerant people can be helped by taking a lipase supplement, but the fat intolerance problem still exists. (i.e …. Taking a food combination containing lipase will gradually reduce the size of gall stones, thus reducing symptoms, but this does not cure fat intolerance just as surgery does not cure disease.) The lipase will help prevent an aggravated condition ONLY if the fat intolerant person minimizes fat consumption. Lipase deficient people have decreased cell permeability, meaning nutrients cannot get in and the waste cannot get out of the cell. For example, diabetics are lipase deficient and cannot get glucose into their cells, and wastes or unwanted substances cannot get out. People with ‘hidden viruses” that are often diagnosed with “Chronic Fatigue Syndrome” also fall into this category. Lipase modulates cell permeability so that nutrients can enter and wastes can exit. Of course, waste-eating enzymes (such as protease) must be taken to help cleanse the blood of the unwanted debris. A common symptom of lipase deficiency is muscle spasms. This is not the “muscle cramp” (tetany) resulting from low ionized blood calcium. It commonly occurs as trigger point pain in the muscles across the upper shoulders, but it can occur in other muscles, such as those in the neck or anywhere in the small or large intestines including the muscles of the rectal tissues. If chronic muscle spasms keep you going back to a chiropractor, osteopath or acupuncturist for repeated adjustments or therapy, try adding some lipase to your diet. It may help you hold your adjustments.People with “spastic colon” may be lipase deficient. They are given toxic muscle relaxant drugs to control the symptoms, but what they really need is a simple food enzyme called lipase. ~~~The condition of vertigo, or labrynthis, also called Meniere’s Disease (dizziness aggravated by movement such as walking or driving), can result from lipase deficiency. A nutritionist saw this condition develop suddenly in a young man after the typical American fat challenge test – a meal which consisted of a fried fish sandwich with tartar sauce, double cheeseburger plus a bag of french fries. The dizziness was accompanied by severe nausea and vomiting which was aggravated by movement. This condition lasted several days. Lipase can relieve a condition like this, often within minutes. The condition of menopause is often associated with lipase deficiency because lipase addresses the gonadal tissue. However, PMS is more often associated with protease deficiency.

~~~CELLULASE DEFICIENCY CONDITIONS: Our body makes no cellulase at all, whereas our pancreas produces enzymes similar to protease, amylase and lipase. They are similar, but not identical, because ONLY FOOD ENZYMES WORK IN THE STOMACH. Pancreatic enzymes work in the duodenum when it is at the right alkaline pH (third part of digestion). Because our bodies do not make cellulase, this food enzyme is essential. We must eat it on a daily basis. Remember, ONLY RAW FOODS contain cellulase. Of all the enzymes, this deficiency carries with it the most categories of problems. Cellulase deficiency is a malabsorption syndrome (impaired absorption of nutrients, vitamins, or minerals from the diet by the lining of the small intestine) with its many symptoms of lower abdominal gas, pain, bloating and problems associated with the jejunum and pancreas. Other conditions associated with cellulose deficiency include nervous system conditions such as Bell’s Palsy, Tic and facial neuralgia, all of which respond remarkably to cellulase. Certain toxic conditions, such as chemicals, drugs and toxic metals, including silver amalgam fillings (mercury in the teeth) are greatly alleviated with cellulase. This also includes acute food allergies. People who have malabsorption syndrome and cellulose deficiency have a tendency toward sugar and/or gluten intolerance.

~~~SUCROSE INTOLERANCE: This condition exists when people cannot split the sucrose disaccharide into its twin partners, two units of glucose. Glucose is a primary brain food so expect mental and emotional problems in people who cannot get glucose into the brain. These symptoms include the whole gamut from depression and moodiness to panic attacks, manic and schizophrenic behavior and severe mood swings, which often lead to toxic behavior- modifying drugs. Seizures, cranial problems and headaches in sucrose intolerant people have been observed, not to mention the symptoms of B-vitamin deficiency resulting from the use of refined white sugar. One researcher has observed almost a universal intolerance syndrome among childhood asthmatics. Whether from genetic intolerance or over consumption, the symptoms are the same. Do not be fooled by thinking that refined white sugar is the only culprit and that other synthetic sugars are okay. Many people do not think that such synthetic sugars as corn syrup, fructose, Nutrasweet, saccharin, Sorbital and Mannitol are harmful. However, severe health problems have occurred from one or all of these as well.

~~~LACTOSE INTOLERANCE: People who are intolerant of lactose also have classic symptoms which include abdominal cramps and diarrhea. Other allergic symptoms have been recorded, not the least of which was asthma, from the ingestion of lactose-containing products. You should know that the FDA allows the addition of lactose as a food additive without labeling. Do not think that your children are safe if they are lactose intolerant just because they do not drink milk.


~~~GLUTEN INTOLERANCE: Gluten intolerance is associated with Celiac Disease and Malabsorption Syndrome. It is also associated with Crohn’s Disease. The insidious thing about gluten intolerance is that it creates a sugar intolerance because when gluten intolerant people eat food containing gluten, the brush border cells of the jejunum are injured and thus unable to secrete the disaccharidases (sucrose, lactase and maltose) leading to sugar intolerance. Double Trouble! Most gluten intolerant individuals usually do not need to abstain from all the gluten grains (wheat, oats, rye and barley). However, sometimes it is a must.

 You can find The ariginal information HERE Check out Tony’s site there is LOTS of information! or keep popping back to this site and  educate yourself to good health and longevity!


Modified probiotics may help to fight fat: Study

Modified probiotics may help to fight fat: Study

By Nathan Gray, 23-Dec-2010

Related topics: Research, Probiotics and prebiotics, Weight management

Probiotic bacteria strains tailored to express produce conjugated linoleic acid (CLA) may be able to modify fat tissues, and could play a role in the prevention and treatment of obesity, according to new research in mice.

The study, published in Microbiology, produced Lactobacillus probiotics that were specially designed to express a CLA producing enzyme from other bacteria. The researchers said that their findings could lead to specialised probiotics that have a role in the prevention or treatment of weight management issues.

“These data demonstrate that a single gene (encoding CLA isomerase) expressed in an intestinal microbe can influence the fatty acid composition of host fat,” said the researchers, from the Alimentary Pharmabiotic Centre (APC), Cork, Ireland.

The scientists successfully cloned and overexpressed a gene known to produce CLA from Propionibacterium acnes in Lactococcus lactis bacteria, resulting in a probiotic strain that achieved conversion rates of more than 50 percent of linoleic acid to t10, c12 CLA – a specific type of CLA known to be beneficial in fat tissues.

“To our knowledge the first report to demonstrate that oral administration of a genetically modified t10, c12 CLA-producing strain (containing the single gene for t10, c12 CLA production) results in modulation of the fatty acid composition of the host, including significantly higher concentrations of t10, c12 CLA in adipose tissue, which is directly attributable to the presence of the t10, c12 CLA isomerase gene,” said the researchers.

Good bacteria

The authors noted that evidence is emerging to support the concept that the microbiota can have “profound effects on human health and disease, involving complex host–bacteria interactions that are as yet poorly understood.”

They noted that the gut microbiota is important to the host with regard to metabolic functions, providing nutrients and may offer some resistance to bacterial infections. In addition, the microbiota has been shown to have an effect on disease processes outside the gut.

“CLA has already been shown to alleviate non-alcoholic fatty liver disease that often accompanies obesity. Therefore, increasing levels of CLA in the liver by ingestion of a probiotic strain is of therapeutic relevance,” said Dr Catherine Stanton one of the lead authors of the study.

“Furthermore, fat is not an inert layer around our bodies, it is active and pro-inflammatory and is a risk factor for many diseases, including cancers. The work shows that there is potential to influence this through diet-microbe-host interactions in the gut,” she explained.

Study details

The researchers investigated whether the recombinant Lactobacillus, expressing CLA isomerase from Propionibacterium acnes could influence the fatty acid composition of bodily tissues in a mouse model.

Linoleic-acid-supplemented diets were fed in combination with either a recombinant t10, c12 CLA-producing Lactobacillus or a control strain, to mice for 8 weeks.

Stanton and colleagues reported that ingestion of the strain expressing the CLA isomerase was associated with a 4-fold increase in t10, c12 CLA in the fat tissues of mice when compared with mice that received the non-CLA-producing strain.

“This study demonstrates that t10, c12 CLA production occurred in vivo when a recombinant

Lactobacillus strain harbouring the gene encoding t10, c12 CLA isomerase was administered to mice,” they said.

“We need to further investigate the effects of CLA-producing bacteria on human metabolism, but our work so far certainly opens up new possibilities for the use of probiotics for improvement of human health,” added Dr Stanton.

“It is possible that a CLA-producing probiotic may also be able to keep colon cancer cells in check. All our findings to date demonstrate that the metabolism of gut bacteria can modulate host cell activity in ways that are beneficial to the host,” she said.

Source: Microbiology
Published online ahead of print, doi: 10.1099/mic.0.043406-0
“Recombinant lactobacilli expressing linoleic acid isomerase can modulate the fatty acid composition of host adipose tissue in mice”
Authors: E. Rosberg-Cody, C. Stanton, L. O’Mahony, R. Wall, F. Shanahan, E.M. Quigley, G.F. Fitzgerald, R.P. Ross

Phytopharm CEO insists Hoodia still ‘interesting’ despite patent disposal

Phytopharm CEO insists Hoodia still ‘interesting’ despite patent disposal

Post a commentBy Ben Bouckley, 08-Dec-2010

Related topics: Industry, Phytochemicals, plant extracts, Weight management

Phytopharm ceo Tim Sharpington insists that Hoodia remains an ‘interesting’ functional food ingredient, despite confirming that the firm has returned its production patents to the South African government scientific body it has leased them off since 1995.

Yesterday’s confirmation to marks the end of over 2 years of press speculation that marked the fall-out from the break-down of the UK life sciences firm’s tie-up with Unilever to commercialise a Hoodia-based weight-management product, after which it insisted it was pursuing negotiations with other major players to further work on its concentrated plant extract.

Unilever safety concerns

Hoodia gordonii is a rare South African succulent widely sold as a satiety-inducing supplement that leaves those who take it with the feeling of fullness, but safety concerns about fake hoodia supplements and other issues have tarnished the plant’s image.

From 1995 Phytopharm leased an exclusive patent from the South African government to isolate, extract and synthesise the steroidal glycoside molecule ‘P57’ first developed in a powder form by the latter’s scientists, which is widely believed to be responsible for the plant’s appetite suppressing effects.

In December 2004 the firm then entered into a joint partnership with Unilever to develop a P57-based SlimFast shake, only for the drugs giant to exit the relationship in late 2008 citing “safety and efficacy” issues, where the shake format was rumoured to cause digestive problems since it was metabolised too quickly.

Co-operation deal signed

Phytopharm revealed in its recent preliminary full-year results announcement that it had signed a “co-operation agreement…with the Centre for Scientific and Industrial Research (CSIR) South Africa, which will fund the future development and commercialisation of Hoodia Gordonii as an appetite suppressant.”

“The CSIR, one of the leading research institutions in Africa, is now responsible for further development and commercialisation of Hoodia Gordonii for the management of obesity.”


Sharpington told last night that the deal was a co-operation ‘agreement’ in the full sense, stressing that it is neither a full rights sale nor a standard licensing deal, given that “we licensed it [P57] through the CSIR in the first place”.


Phytopharm would provide the CSIR with technical and research expertise, he explained, adding: “The CSIR originated the patents, and we licensed the intellectual property rights – so we’re giving them back the original patent rights and some other rights in return for a share in future commercialisation income.”

Exiting functional foods

Asked whether he still thought Hoodia had a future a functional ingredient, Sharpington said: “It’s an interesting product, but it still needs some development work. The early Unilever work on solid formulations showed promise, but then they chose to pursue a liquid form and certain issues arose.”


“If it were my choice – and this is just a personal opinion – then I would be pursuing solid formulations, but I can tell you that the CSIR is very committed to the programme.


Sharpington added: “It’s important to stress that we have not lost faith in Hoodia,” before adding that the patent disposal formed part of a “corporate decision to exit the functional foods business” to focus on Phytopharm’s “exciting” pharmaceutical pipeline.

The Glycemic Index Revisited – By Dr Mike Roussell


The Glycemic Index Revisited

by Dr. Mike Roussell – 12/03/2010
 Original article on T-Nation HERE

I’m sure that you can appreciate the importance of optimizing your blood sugar levels; not only for the quest of a lean, muscular physique but, as the opening quote illustrates, the pursuit of good health and a longer life.

But considering that walking around with a glucometer and sticking ourselves after every meal just isn’t practical – or polite – a more efficient method of measuring the effect of carbohydrates on blood sugar levels needed to be determined.

Unfortunately, what athletes, bodybuilders, and TNation readers find scientifically relevant usually doesn’t find its place on the National Institute of Health’s “Top 10 Research Programs to Give Funding To” list.

Sometimes though, we get lucky, and while it wasn’t with the NIH, the British Diabetic Association and the Medical Research Council decided in the late 1970s to find out more about the differing effects of carbohydrate-based foods on blood sugar.

Fast forward to 1981, and the Glycemic Index (GI), a method of ranking the effects of different carbohydrate based foods on blood sugar, was born.

The GI of a food is measured in a two-step process. Researchers will give a person 50 grams of pure glucose and then measure their blood glucose levels over the course of several hours. This pure glucose serves as the control, as theoretically, nothing can be digested faster than pure glucose.

Next, researchers give the same person 50 grams of the food in question (like carrots, rice cakes, or black beans), and measure their blood glucose levels for several hours afterwards. As the diagram on the right and the following technical definition of the GI shows, the blood sugar responses for the two foods are then compared.

One key component to how the GI is measured has to do with amount. The amount of food used is always the same, 50 grams. As a result, the GI only takes into account the type of carbohydrate and not the amount. This is a point of criticism that many GI critics often bring up; for example, how practical is the GI when 50 grams of carbs from rice can be ingested with ease while 50 grams from carrots would require Bugs Bunny-like dedication?

The Glycemic Load

To make the GI more real world applicable – as no one eats food in 50-gram increments – scientists came up with the Glycemic Load (GL). The GL is a carbohydrate/blood sugar rating that accounts for both type and amount of carbohydrate.

It’s defined by this equation:

Here’s an example of how the GL works versus the GI:

Food Standard Serving Size Glycemic Index Glycemic Load
Jasmine rice 150g 99 42
Carrots 80g 47 3
Apple 120g 34 5

Traditionally, the much-maligned carrot is vilified by GI disciples because they have a higher GI than most vegetables (one study found the GI of carrots to be 90 but these findings were never replicated), but as you can see the average GI for carrots is only 47 – which actually makes carrots a low GI food – and when you take into account the amount most non-hares would normally eat, the GL for carrots is really very low.

The GI is a property of a food, just like the amount of protein or fat in a food, while the GL refers to the composition (type of carbohydrate) and size of your meal (amount of carbohydrate).

Dr. Wolever, an Oxford trained physician, nutrition PhD, and world leading expert on the Glycemic Index, hammered this point home repeatedly in a seminar I attended recently. This is an important designation, as it makes a food’s GI rating applicable across different populations.

The Insulin Index

You might have heard about a study published over a decade ago talking about the Insulin index. Like the GL, the idea behind the Insulin Index is that scientists wanted to quantify the effects that different foods had on insulin levels.

But one problem with the Insulin Index is that the insulin response can vary tremendously between individuals, thereby requiring a lot of extra data on the effects of different foods in a variety of populations to have a standardized version of the Insulin Index.

To further complicate matters, the Insulin index concept never really took off in the scientific community – at the time of writing this article, there were 22 times more scientific papers in PUBMED about the GI compared to the Insulin Index.

Now that we’ve established the various indexes, let’s see how you can best apply them to your physique pursuits. Here are two important points:

I always stress this point with clients when we discuss carbohydrates, blood sugar, and the Glycemic Index. Generally (and practically) speaking, foods with a low GI will also have a low GL.

Green leafy vegetables have a low GI, and while you can eat a large volume of these foods, the actual gram amount of carbohydrate that you’re consuming will also be low (making the GL low as well), while foods with a higher GI are usually more carbohydrate dense (meaning that if you eat a large volume of these foods, you’ll also be eating a lot of carbohydrates).

Long story short: Meals with low glycemic carbs will naturally have a lower GL and meals with higher glycemic carbs will naturally have a higher GL. Why make it more complicated than it has to be?

Another point of criticism regarding the GI is consistency. While the measuring of a food’s GI is supposed to be a standardized procedure, different labs have calculated different GI’s for the same food. While this might sound like a problem, it really isn’t. Why?

As you can see by the chart below, when using the GI to categorize foods, three main categories are used: High, medium, and low.

High GI Foods Medium GI Foods Low GI Foods
Shredded Wheat Apricots Green Vegetables
Bagel Long Grain Rice Nuts
White or Whole Wheat Bread Pita bread Apples
Couscous Raisins Barley
Cornflakes Brown Rice Oranges
Rice Cakes Pineapple Strawberries
Pancakes     Corn Tortilla

If you follow my recommendations and use the GI as a tool to improve your carbohydrate choices, high versus low GI is what really matter. When researchers combined discrepancies found between laboratories and published studies, low GI foods were always low GI foods and high GI foods were always high GI foods.

Jasmine rice and rice cakes don’t suddenly become low GI foods simply because two labs can’t agree on a score.

The Glycemic Index of Foods Can Change

Remember when I mentioned above that the GI of a food was a property of the food? After reading that, you might’ve thought that means that the GI rating of a food always stays the same. Unfortunately, that’s not always the case due to some interesting food science – and more recently, the unrelenting efforts of food companies to get ‘whole grains’ into our diets.

There are three common ways that the GI of a food can change: processing, ripeness, and cooking. Let’s take a look at how cooking can influence the GI.

The Potato Story

This is where it gets really cool. Let’s say you take a potato; prepare and eat it two different ways and it’ll have two different GI ratings.

Raw potatoes, cooked potatoes, and potatoes that are cooked and then cooled all have different GI ratings due to the potato’s unique starch make-up. Certain types of potatoes, like red potatoes, contain high levels of amylose. When cooked, amylose is released, mixes with water molecules and forms a gel like substance. By letting the potatoes cool, you’re giving the gel a chance to solidify into a state that’s more resistant to digestion. If you eat it while it’s still hot, the gel is still gelling, and it will get digested faster.

Lest you think this is the spud-inspired version of splitting hairs, think again: according to one researcher I talked, to the difference between eating a warm potato versus waiting for it to cool and then eating it can be a GI rating of 75 versus 40!

Who would have thought that potato salad could be better for you than a steaming baked potato?

Here’s a muscled-up version of potato salad for you to try:

  • 3 medium red potatoes
  • 1/2-cup olive oil mayonnaise
  • 5 chives, minced
  • 2 strips turkey bacon (not the processed Jennie-0 stuff that looks like play-dough pressed into a bacon form – try Applegate Farms)
  • 1/2 medium onion, diced
  • 1 stalk celery, diced
  • 1 Tbsp yellow mustard

How to Prepare:

Place the potatoes in a medium-sized pot with boiling water. Cook for ~15 minutes, until the potatoes are fork tender. While the potatoes are cooking, cook the turkey bacon in a nonstick frying pan over medium heat. Once the potatoes are cooked, remove them from the pot and let cool.

Next, dice up the turkey bacon and place in a bowl with the mayonnaise, chives, onion, celery, and yellow mustard. When the potatoes have cooled, cut them up into 1-inch cubes. Add to the bowl and mix thoroughly. Add salt, pepper, and Frank’s Red Hot to your desired taste. Makes 2 servings (see nutrition facts below).

Enjoy this with a roasted chicken breast or grilled flank steak for a great post training meal.

Protein and Carbohydrate Affects on Glycemic Index & Glucose Response

Another criticism of the reliability and effectiveness of the GI is that it ranks foods by themselves, when in reality, when we eat carbohydrate-based foods, we eat them together with protein and fats.

Another factoid I frequently hear bandied about is that “adding protein and fats to a meal reduces the GI of rice/potato/Pop Tarts/etc.”

However, as stated earlier, one of the important points about the GI rating is that it’s a property of the food, so adding fat and protein to a meal containing white rice for example doesn’t change the GI of rice, it only will reduce the rise in blood sugar…or will it?

In 2006, Dr. Wolever published a study that was the first to systematically examine the ‘mixed meal’ question. In this study, participants received shakes containing glucose (50 grams), protein (0, 5, 10, or 30 grams), and fat (0, 5, 10, or 30 grams).

The researchers found that gram-for-gram, protein had almost a three times greater effect than fat at reducing glucose response to the meal. They also found that the effect of protein was linear across the protein dosages (0 grams to 30 grams), so that the more protein that was in the shake, the greater the reduction in glucose response.

Dr. Wolever cautioned against taking these findings out of context, as the study used liquid shakes and not whole food meals. But as a TNtaion reader who probably has a second pantry dedicated to tubs of Metabolic Drive, this research is especially relevant to you.

To further explore the ‘mixed meal’ question, Dr. Wolever ran another study, this time using whole food meals. The meals contained 0-18 grams of fat and/or protein and 16-79 grams of carbohydrates (with GI’s ranging between 35-100).

They found very different results than the previous smoothie study: when using whole foods, the protein and fat content of the meals had a negligible effect on glucose levels. The total carbohydrate content of the meal and the GI of the foods in the meal were able to predict glucose response with almost 90% accuracy.

While they might have found different effects at higher protein dosages, when these two studies are taken together the message is pretty clear: if you’re having a shake, then adding protein to that shake is a good way of controlling your blood sugar response.

If you’re having a whole food meal, then eating low glycemic carbs and reducing your total carb intake (which can be done by eating low glycemic carbs) is the best way to control your blood sugar response.

Glycemic Index, Nutrition Timing, and Your Diet

What’s the best way to use glycemic index in your diet? You can use the glycemic index to optimize the nutrient timing of your diet.

Phase AM Workout/Post Workout PM
Hypertrophy Phase High + Medium GI carbs Mainly High GI carbs Low & Medium GI carbs
Maintenance Phase Low + Medium GI carbs Mainly High GI carbs Low GI Carbs
Fat Loss Phase Low GI carbs Mainly High GI carbs Low GI carbs

The Glycemic Index Wrap Up