Digestive Disorders Protocol

The pancreas and liver are digestive organs that produce most of the body's digestive enzymes. The remainder should come from uncooked foods, such as fresh fruits and vegetables, raw sprouted grains, seeds and nuts, unpasteurized dairy products, and enzyme supplements.

Food in its natural, unprocessed state is vital to the maintenance of good health. The lack of it in the modern diet is thought to be responsible for degenerative diseases. Cooking food, particularly for long periods of time and at more than 118°F, destroys enzymes in food and leaves what is often consumed in today's enzyme-less diet. This is one reason why, by middle age, we may become metabolically depleted of enzymes. Our glands and major organs suffer most from this deficiency. The brain may actually shrink as a result of an overcooked, overly refined diet that is devoid of enzymes desperately needed by the body. In an effort to meet the deficiency, the pancreas may swell. Laboratory mice fed heat-processed, enzyme-less foods develop a pancreas two or three times heavier than that of wild mice eating an enzyme-containing natural diet of raw food.

When food is consumed uncooked, fewer digestive enzymes are required to perform the digestive function. The body will adapt to the plentiful, external supply by secreting fewer of its own enzymes, preserving them to assist in vital cellular metabolic functions. One of the worst cooking methods is frying, since frying results in much higher temperatures than boiling. Frying damages protein as well as destroying enzymes.

Enzymes can also be wasted by lifestyle factors. Enzymes work harder with increasing temperatures and are used up faster. A fever, for example, induces faster enzyme action and is therefore unfavorable for bacterial activity. Enzymes can be found in urine after a fever and also may be found after strenuous athletic activity.

A natural behavior of animals is to harness the power of enzymes in food by burying or covering their food, allowing enzyme activity to start predigesting the food. By this natural behavior, animals instinctively preserve their own enzyme supply. Similarly, people of some native cultures also preserve their enzyme supply and prevent disease through efficient use of enzymes. Whales have up to 6 inches of fat to keep them warm, but their arteries are not clogged. Eskimos, who frequently consume large quantities of fat, are often not obese. Both of these groups eat the fat-digesting enzyme lipase in the form of raw foods.

Studies (both in vitro and controlled in vivo) using internal and parenteral routes have examined the effectiveness of many different types and sources of plant enzymes in several conditions, including poor digestion, poor absorption, pancreatic insufficiency, steatorrhea, lactose intolerance, celiac disease, obstruction of arteries, and thrombotic disease.

Enzymes from the Aspergillus oryzae fungus were subjected to numerous studies, evaluating their role in supporting healthy digestion. Additionally, human studies suggest the proteolytic enzymes derived from A. oryzae fungus may play a role in anti-inflammatory and fibrinolytic therapies. The enzymes appear to be relatively stable in heat, and they are also active throughout a wide pH range. This is important because most enzymes are deactivated in stomach acid. These enzymes are synthesized from fungus but contain no fungal residue even though that is their derivation. Modern filtration techniques and technology enable these fungal enzymes to be well suited for human consumption.

According to Dr. Mark Percival (1985), the oral supplementation of digestive enzymes taken just before or at mealtime can assist digestion. Even though most supplemental enzymes are labile and will deactivate when exposed to stomach acid, Dr. Percival believes some of the enzymes will remain active if they are taken with a meal or just before. Percival says, "The enzymes are physically protected" by the meal and allow some enzymatic activity to occur in the stomach. The enzymes that get through to the small intestine may help with digestion there as well. pH plays a major role in enzymatic activity, therefore, the enzymes derived from Aspergillus "may be highly useful as they appear to be remarkably stable, even when subjected to an acidic environment." Dr. Edward Howell (1986) adds that he chews an enzyme capsule with his food in order to start the digestive process as soon as the food is consumed since enzyme activity has been shown to begin even before the food is swallowed.

As early as 1947, Dr. Arnold Renshaw (Manchester, England) reported in Annals of Rheumatic Disease that he had obtained good results with enzyme treatment of more than 700 patients with rheumatoid arthritis, osteoarthritis, or fibrositis: "Some intractable cases of ankylosing spondylitis and Still's disease have also responded to this therapy." He said that of 556 people with various types of arthritis, 283 were much improved, and 219 were improved to a less marked extent; of 292 people who had rheumatoid arthritis, 264 of them showed several degrees of improvement. More time was required before improvement was seen when the duration of the disease had been long-term, although most people started to show some improvement after only 2 or 3 months of enzyme therapy. In spite of these favorable findings, digestive enzyme therapy has been reserved for diseases that directly result in a pathological deficiency of pancreas-derived digestive enzymes.

According to Schneider et al. (1985), common digestive disorders may benefit from enzyme replacement. Oral intake of exocrine pancreatic enzymes is of key importance in the treatment of maldigestion in chronic pancreatitis with pancreatic insufficiency. Schneider studied the therapeutic effectiveness of a conventional and an acid-protected enzyme preparation and an acid-stable fungal enzyme preparation in the treatment of severe pancreatogenic steatorrhea. The results showed that a supplemental enzyme preparation is best for patients with chronic pancreatitis and those who underwent Whipple's procedure (a surgical procedure performed on pancreatic cancer patients), while patients with an intact upper GIT do best with an acid-protected porcine pancreatic enzyme preparation.

Rachman (1997) reported that 58% of the population has some type of digestive disorder and that lack of optimal digestive function associated with enzyme inadequacy may lead to malabsorption and other related conditions. In the elderly, the problem is often exacerbated because the elderly may have suboptimal production of gastric hydrocholoric acid. "This can be a significant factor that can impact nutrient absorption along with the creation of maldigestive-type symptoms. Bacterial production of hydrogen and methane are determined after a carbohydrate challenge. Excessive levels of these gases reflect overgrowth of bacteria in the upper gut." Rachman suggests there may be improvement with enzyme replacement. He also adds that enzymes taken orally at meals may improve the digestion of dietary protein, thereby decreasing the quantity of antigenic macromolecules that leak across the intestinal wall into the bloodstream. Such leaking may trigger the body's defenses against what it perceives to be foreign protein or polypeptide invaders, producing the symptoms of allergies.

Howell (1986) also agrees that allergies can respond to adding enzymes to the diet. He also says excessive cholesterol levels can respond to dietary enzymes as well. Howell quoted a 1962 study by three British doctors (C.W. Adams, O.B. Bayliss, and M.Z. Ibrahim), who set out to discover why cholesterol clogs arteries, ultimately manifesting in heart disease. They found that all enzymes studied became progressively weaker in the arteries as people aged and the hardening became more severe. They suggested a shortage of enzymes is part of the mechanism that allows cholesterol deposits to accumulate in the inner part of arterial walls. As early as 1958, researcher L.O. Pilgeram conducted blood tests at Stanford University and demonstrated a progressive decline of lipase in the blood of atherosclerotic patients in advancing middle and old age.

About the same time, researchers at Michael Reese Hospital in Chicago found that enzymes in the saliva, pancreas, and blood became weaker with advancing age and speculated that fat may be absorbed in the unhydrolyzed state in atherosclerosis. They also found definite improvement in the character of fat utilization following the use of enzymes.

Intravenous (IV) administration of brinase, a proteolytic enzyme prepared from A. oryzae, was found by FitzGerald et al. (1979) to be beneficial in treating chronic arterial obstruction. Patients were observed for 3 months before they were given six IV infusions of either saline or brinase for more than 2 weeks. No changes were observed during the observation period. After infusion, resumed blood flow was found in 17 of 27 obstructed arterial segments. The number of patent segments increased from 11 to 27. No improvements were observed in the patients who were treated with placebos.

Pancreatin is secreted from the pancreas. It provides potent concentrations of the digestive enzymes protease, amylase, and lipase and is sold as a drug to treat those with pancreatic insufficiency. Pancreatin efficacy was demonstrated in a study conducted on patients taking pancreatin to maintain postoperative digestion. The effects of supplementation were determined by measuring the postoperative intestinal absorption and nutritional status in a randomized trial. The patients received pancreatin or a placebo. Before the trial, patients showed abnormal digestion of fats and protein. Total energy was low at baseline and at 3 weeks after surgery. Supplementation with pancreatin improved fat and protein absorption as well as improving nitrogen balance. However, those patients taking a placebo had worsened absorption after surgery. These data suggest that long-term, postoperative pancreatic enzyme supplementation is both effective and necessary in surgery patients who had pancreatitis.

Considerable evidence exists in support of the beneficial effects of enzymes, both natural and supplemental. Plant enzymes have shown obvious benefit for specific conditions. Research with intact absorption of food substrates has shown that nondigested food substrates enter the blood and that plant enzymes break down different food substrates that would otherwise have been passed into the blood partially digested.

Youth is the time of life when our normal ability to produce enzymes is greatest. It is also a time of rapid growth and often a time with no serious illness. As people age and their food enzymes become depleted, they often begin to suffer a broad range of health complaints.

According to Howell (1986), how long we live and our state of health are determined by our enzyme potential. Howell referred to a study by Meyer and associates at Michael Reese Hospital in Chicago that reported that the presence of enzymes in the saliva of young adults is 30 times higher than that in people over 69 years of age.

Therefore, humans consuming an enzyme-less diet use vast quantities of their enzyme potential from secretions from the pancreas and other digestive organs, perhaps resulting in shortened lifespan, illness, and lowered resistance to all types of stress.

In the early 1970s, G.A. Leveille, a University of Illinois researcher, discovered that enzyme activities in the tissues become weaker with age. Leveille conducted experiments on rats and found that at the age of 18 months--considered to be old for rats--when on enzyme-free fabricated diets, enzyme activity shrunk to less than 20% of its level at one month of age. Howell (1986) agrees: "The more lavishly a young body gives up its enzymes, the sooner the state of enzyme poverty, or old age, is reached."

The answer is to substitute raw foods for cooked foods as much as possible. Howell (1986) recommends that we eat foods with their enzymes intact and supplement cooked foods with enzyme capsules. He suggests we can stop abnormal and pathological aging processes. Howell singles out raw milk, bananas, avocados, seeds, nuts, grapes, and other natural foods as rich in food enzymes. He also suggests that an enzyme supplement be taken with all cooked food. Under medical supervision, Howell suggests large doses of enzyme therapy to treat certain diseases.

Few would disagree with the old adage that "we are what we eat," but it is not quite that simple. Enzymes make the digestion of food possible. This means we must make maximum use of enzyme activity, both internal enzymes and those consumed either in food or as supplements.

Benefits of Artichoke for Digestive Disorders

The artichoke plant is best known for its heart, the bottom part of its spiky flower bud that many of us have learned to appreciate as both a delicacy and a nutritious vegetable. However, other parts of this tall thistle-like plant, which never reach the dinner table, have proven to be even more beneficial for our health. Clinical studies show its large basal leaves to be effective for improving digestion and liver function, as well as cholesterol levels.

Since ancient times, humans have looked to nature for help to cure diseases. Up until modern times, most remedies were derived from the plant kingdom, and even today a large percentage of our current pharmaceutical drugs are based on plant extracts from various parts of the world. Many old herbal remedies, however, have fallen into oblivion with the development of modern medicine.

Artichoke extract is one of the few phytopharmaceuticals whose experiential and clinical effects have been confirmed to a great extent by biomedical research. Its major active components have been identified, as have some of its mechanisms of action in the human body. In particular, antioxidant, liver-protective, bile-enhancing, and lipid-lowering effects have been demonstrated, which correspond well with the historical use of the plant. More research is needed to determine in detail the mechanisms of action for these effects. However, there appears to be enough evidence to suggest a potential role for artichoke extract in some areas where modern medicine does not have much to offer.

Used as a food and a medical remedy as early as 400 bc, the artichoke plant has a long history. At the time, a pupil of Aristotle by the name of Theophrastus was one of the first to describe the plant in detail. Enjoyed as a delicacy, an appetizer, and a digestive aid by the aristocracy of the Roman Empire, it later seemed to fall into oblivion until the 1500s, when medicinal use of the artichoke for liver problems and jaundice was recorded. In 1850 a French physician successfully used extract of artichoke leaves in the treatment of a boy who had been sick with jaundice for a month and had made no improvement from the drugs used at that time. This accomplishment inspired researchers to find out more about the effects of this extract, and their research resulted in the knowledge we have today about the extract and its mechanisms of action.

Artichoke leaf extract is made from the long, deeply serrated basal leaves of the artichoke plant. This part is chosen for medicinal use because the concentration of the biologically active compounds is higher here than in the rest of the plant. The most active of these compounds have been discovered to be the flavonoids and caffeoylquinic acids. These substances belong to the polyphenol group and include chlorogenic acid, caffeoylquinic acid derivatives (cynarin is one of them), luteolin, scolymoside, and cynaroside.

Cynarin was the first constituent of the extract to be isolated in 1934. Interestingly, it is found only in trace amounts of fresh leaves but is formed by natural chemical changes that take place during drying and extraction of the plant material. Cynarin was originally believed to be the one active component of the extract. Today the whole complex of compounds is considered important, since it has not yet been completely clarified which component is responsible for each effect. It is claimed that neither cynarin alone, nor fresh plant material achieves the potency of the dried total extract (Kirchhoff et al. 1994).

Chlorogenic acid, another major component of the artichoke leaf extract, has recently become known as a powerful antioxidant with exciting potential in many applications. Laboratory investigations are ongoing all over the world with promising findings for future clinical application in areas such as HIV, cancer, and diabetes.

Most of the modern research on artichoke has been done with the German artichoke extract Hepar SL Forte, standardized to contain 3% caffeoylquinic acids. A new, even more potent extract, standardized at 15% caffeoylquinic acids--calculated as chlorogenic acid--is now available on the American market.

Biological Effects
The original uses of artichoke since ancient times have been as an aid for indigestion and insufficient liver function. The mechanism of action, however, has been essentially unknown. Recent findings have provided a new foundation for our understanding and discovered additional benefits of the extract, such as antioxidant and lipid-lowering effects.

Digestive Disorders Protocol Pg (1) (2) (3) (4)

These statements have not been evaluated by the FDA. These products are not intended to diagnose, treat, cure, or prevent any disease