Steps To A Healthier Digestive System
Elimination diets are a good method of determining what foods cause an allergic reaction in the GI tract lining. Planning and following such diets are a safe starting point for anyone desiring to track their GI tract response to food. Interview physicians to learn who may be most qualified to assist in planning an elimination diet. A very good indicator of a healthy GI tract is regular transit time for complete food digestion. Patients who are regular are usually in optimum GI health.
Aging causes many people to experience problems with digestion. It is estimated that after age 40 there is an approximate decrease of 20-30% in the body's ability to produce enzymes. The use of specific enzymes can help improve the efficiency of digestion. Enzymes can be used to enhance the proper breakdown of foods in order to more properly digest, absorb, and utilize nutrients.
Enzymes Are a Vital Component of the Digestive Process
Enzymes are essential to the body's absorption and utilization of food. The capacity of the living organism to make enzymes diminishes with age, and some scientists believe that humans could live longer and be healthier by guarding against the loss of our precious enzymes.
Enzymes are responsible for every activity of life. Even thinking requires enzyme activity. The two primary classes of enzymes responsible for maintaining life functions are digestive and metabolic. The primary digestive enzymes are proteases (to digest proteins), amylases (to digest carbohydrates), and lipases (to digest fats). These enzymes function as a biological catalyst to help break down food. Raw foods also provide enzymes that naturally break down food for proper absorption. Metabolic enzymes are responsible for the structuring, repairing, and remodeling of every cell, and the body is under a great daily burden to supply sufficient enzymes for optimal health. Metabolic enzymes operate in every cell, every organ, and every tissue, and they need constant replenishment.
Digestion of food takes high priority and has a high demand for enzymes. When we eat, enzymatic activity begins in the mouth, where salivary amylase, lingual lipase, and ptyalin initiate starch and fat digestion. In the stomach, hydrochloric acid activates pepsinogen to pepsin, which breaks down protein, and gastric lipase begins the hydrolysis of fats. Without proper enzyme production, the body has a difficult time digesting food, often resulting in a variety of chronic disorders.
Poor eating habits (e.g., inadequate chewing and eating on the run) may result in inadequate enzyme production and, hence, malabsorption of food (which is exacerbated by aging because this is a time of decreased hydrochloric acid production) as well as a general decline in digestive enzyme secretion.
Saliva is rich in amylase, while gastric juice contains protease. The pancreas secretes digestive juices containing high concentrations of amylase and protease, as well as a smaller concentration of lipase. It also secretes a small concentration of maltase, which reduces maltose to dextrose. Animals eating raw food often have no enzymes at all in saliva, unlike humans. However, dogs fed a high carbohydrate, heat-treated diet have been found to develop enzymes in their saliva within a week in response to enzyme-depleting foods.
One of America's pioneering biochemists and nutrition researchers, Dr. Edward Howell (1986), cites numerous animal studies showing that animals fed diets deficient in enzymes have an enlarged pancreas, as huge amounts of pancreatic enzymes are squandered in digesting foods devoid of natural enzymes. The result of this wasteful outpouring of pancreatic digestive enzymes is a decrease in the supply of crucial metabolic enzymes and impaired health.
How significant is an enzyme deficiency to overall health? For starters, organs that are overworked will enlarge in order to perform the increased workload. Those with congestive heart failure or aortic valvular disease often suffer from an enlarged heart. When the pancreas enlarges in order to produce more digestive enzymes, there results a deficiency in the production of life-sustaining metabolic enzymes, as available enzyme-producing capacity is used in digesting food instead of supporting cellular enzymatic functions. The tremendous impact that wasting pancreatic enzymes can have on health, and even life itself, has been established in animal studies. The critical question is how this applies to human health.
For much of the 20th century, European oncologists have included enzyme therapy as a natural, nontoxic therapy against cancer, and almost all leading alternative cancer specialists treating Americans prescribe both food enzymes and concentrated enzyme supplements as primary or adjuvant cancer therapies. A New York City cancer specialist, Nicholas Gonzalez, M.D., uses very high doses of supplemental pancreatic enzymes as a primary antitumor therapy. His clinical successes have led conventional drug companies to seek to duplicate these natural therapies and offer them as adjuvant drug therapies. If pancreatic enzymes are effective in treating existing cancers, one might assume that maintaining a large pool of these enzymes in the body should help prevent cancer from developing. Studies have shown that persons who eat fresh fruits and vegetables (with high levels of natural enzymes) have significantly reduced levels of cancer and other diseases. It has not been proven that the high enzyme content of these foods is partially responsible for their anticancer effect, but the evidence is compelling.
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 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 uncooked food is consumed, 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 and destroys 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 or just before a meal. 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 because enzyme activity has been shown to begin even before the food is swallowed, he chews an enzyme capsule with his food in order to immediately start the digestive process.
As early as 1947, Dr. Arnold Renshaw (Manchester, England) had obtained good results with enzyme treatment of more than 700 patients with rheumatoid arthritis, osteoarthritis, or fibrositis, noting that "some intractable cases of ankylosing spondylitis and Still's disease have also responded to this therapy." He reported 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 (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 a Whipple procedure (a surgical procedure performed on pancreatic cancer patients), while patients with an intact upper GI tract 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 a 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) agrees that allergies can respond to adding enzymes to the diet. He 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 (1979) to be beneficial in treating chronic arterial obstruction. Patients were observed for 3 months before being 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. It 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 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 undigested food substrates enter the blood and 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 the presence of enzymes in the saliva of young adults is 30 times higher than in people over 69 years of age.
Therefore, humans consuming an enzyme-less diet use vast quantities of their enzyme potential from pancreatic secretions 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 receiving 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 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.