Introduction:
An enzyme is any of various types of proteins which act as catalysts to speed up
the body's biochemical processes. Enzymes build new proteins, cells, tissues,
and organs, and can also break down these same tissues. All living organisms
contain enzymes - without them, life could not exist.
Digestive enzymes are a group of specific enzymes in the gastrointestinal tract
which function to break down the components of food. While digestive enzymes are
also produced in the mouth (in saliva) and the stomach, the area of greatest
digestive enzyme activity is in the small intestine.
A key organ in digestive enzyme production is the pancreas. Up to 1.5 quarts of
pancreatic juice, containing digestive enzymes to break down carbohydrates, fat
and protein, is secreted by the pancreas into the small intestine every day. The
major pancreatic enzymes are known as lipases, amylases, and proteases
(including trypsin, chymotrypsin and carboxypeptidase).
Supplemental enzymes, particularly pancreatic digestive enzymes, have a long
history of traditional use.5 In addition to digestive support, pancreatic
enzymes have been recommended for immune system support, to support urinary
tract health, lung health, and for the relief of occasional pain and
inflammation associated with exercise.
How Does It Work?:
Enzymes have specificity, meaning they act only on
their specific substrates. For example, the digestive
enzyme
amylase acts on carbohydrates, lipase on fats, and protease on protein.
Therefore, to obtain greater benefits, a digestive enzyme supplement should
include a range of enzyme types. Mega-Zyme systemic enzymes contains
eight key enzymes, plus 10X pancreatic enzymes for maximum digestive support.
10X strength refers to a high potency (10X) pancreatic enzyme complex which is
10 times more potent than the minimum activity specified by the United States
Pharmacopiea (USP).
The ingredients in Mega-zyme systemic enzymes are buffered with
bicarbonate. Bicarbonates help to neutralize the acid environment of the stomach
and allow the digestive enzymes to work in the small intestine. Normal pH of the
stomach is 2 (acidic) while pancreatic juice is about 8 (basic). Bicarbonates
assist in changing the acidic environment to an alkaline environment.
The bicarbonates in Mega-Zyme systemic enzymes are designed to work with
the other ingredients to support a healthy digestive system.
Mega-Zyme systemic enzymes was also used in several clinical trials
demonstrating its benefits for relieving muscle pain and inflammation associated
with exercise.7-9 In comparison with the placebo group, athletes
taking Mega-Zyme systemic enzymes before and after intense exercise had
less muscle pain and faster recoveries.
The following chart summarizes the activity of each of the enzymes in Mega-Zyme
systemic enzymes.
| Enzyme |
Substrate |
Action |
Source |
| Protease |
Protein |
Cleaves polypeptide chains10 |
Porcine |
| Amylase |
Carbohydrates |
Breaks down starch to maltose and
dextrin11 |
Porcine and
Aspergillus oryzae |
| Lipase |
Lipids (fats) |
Degrades fats to glycerol and fatty
acids12 |
Porcine and
Rhizopus Oryzae |
| Trypsin |
Protein |
Hydrolyzes peptides, amides, esters,
etc at the bonds of the carboxyl groups of L-arginine or L-lysine13 |
Porcine |
| Papain |
Protein |
Catalyzes the hydrolysis of proteins
and peptides with preferential cleavage at bonds containing arginine,
lysine, and glycine residues14 |
Papaya |
| Bromelain |
Protein |
Hydrolyzes proteins to oligopeptides and
amino acids15 |
Pineapple |
| Lysozyme |
Starch (initiates breakdown) |
Hydrolyses the bond between N acetyl
muramic acid and N acetyl glucosamine16 |
Egg |
| Chymotrypsin |
Protein |
Cleaves carboxyl links of hydrophobic
amino acids17 |
Bovine |
References:
1. Pancreas. In: Thomas CL, d. Taber's
Cyclopedic Medical Dictionary. 17th ed. Philadelphia, Pa: F.A. Davis;
1993:1414.
2. Guton AC, Hall JE. Secreotry Functions of
the alimentary Tract. In: Textbook of Medical Physiology. 9th ed.
Philadelphia, Pa: WB Saunders Company; 1996: 824-825.
3. Gastrointestinal Function. In: Porth CM.
Pathophysiology. 5th ed. Philadelphia, Penn: Lippincott-Raven Publishers;
1988:714-715.
4. Enzymes. In: Thomas CL, ed. Taber's
Cylcopedic Medical Dictionary. 17th ed. Philadelphia, Pa: F.A. Davis;
1993:645-655.
5. Cichoke AJ. Pancreatic enzymes. In:
Textbook of Natural Medicine. Pizzorno JE, Murray MT, eds. Edinburgh:
Churchill Livingstone; 1993:857.
6. Whitney EN, Rolfes SR. Digestion,
Absorption, and Transport. In: Understanding Nutrition. 6th ed. St. Paul,
MN: West Publishing Company; 1993:73-74.
7. Miller PC, et al. The effects of protease
supplementation on skeletal muscle function and DOMS following downhill running.
J Sports Sci. 2004 Apr;22(4):365-72.
8. Miller PC, Bailey SP, McInnis KR, Hall EE.
Comparison of protease and NSAID supplementation on muscle soreness and pain
threshold following downhill running. Med Sci Sports Exerc.
2003:35(5Supplement):S197.
9. Miller PC, Bailey SP, Cormier S, Khlebopros
A, Hall EE. Comparison of protease and NSAID supplementation on muscle soreness
and contractile performance following eccentric contractions. Med Sci Sports
Exerc. 2002;34(5):S232.
10. Protease. Department of Plant Pathology
Online Glossary. Cornell University. Available at:
http://ppathw3.cals.cornell.edu/glossary/Defs_P.htm. Accessed June 28, 2006.
11. Amylase. The Merck Index: An
Encyclopedia of Chemicals, Drugs, and Biologicals. Whitehouse Station, NJ:
Merck & Co., Inc.1996:102.
12. Lipase. The Merck Index: An Encyclopedia
of Chemicals, Drugs, and Biologicals. Whitehouse Station, NJ: Merck & Co.,
Inc.1996:941.
13. Trypsin. Stedman's Medical Dictionary,
25th ed. Baltimore: Williams and Wilkins; 1990:1644.
14. Papain. Medical Dictionary. Available at
www.mercksource.com. Accessed June 28, 2006.
15. Bromelain. In: Fleming T, ed. PDRฎ for
Nutritional Supplements. Montvale, NJ: Medical Economics Company;
2001:70-73.
16. Lysozyme. Stedman's Medical Dictionary,
25th ed. Baltimore: Williams and Wilkins; 1990:908.
17. Chymotrypsin. Stedman's Medical
Dictionary, 25th ed. Baltimore: Williams and Wilkins; 1990:306.
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