ENZYME INFORMATION SHEET

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ENZYME INFORMATION SHEET

By Chuck is, BS, B.Ch.

Enzymes are proteinaceous substances of various sizes, molecular weights and

shapes depending on their function. Enzymes serve as catalysts in metabolic

chemical reactions. That is, they serve to speed up specific chemical reactions

by reducing the activation energy for the reaction converting substrates to

products. A complete explanation of enzyme kinetics and the kinetic-molecular

theory is beyond the scope of this paper but a reduction in activation energy

tremendously increases the rate at which these reactions occur by hundreds or

thousands of times.

The functions of enzymes in metabolism are broken down into six broad

categories. These categories are (Conn, Stumpf, et al, p.139, Zubay, pp.265-66):

Hydrolases- Catalyze the breakdown of complex substrates into smaller

segments

Oxioreductases- Catalyze oxidation and reduction reactions

Ligases- Catalyze the combination of two smaller substrates into one large

molecule

Lyases- Catalyze the splitting of double and triple bonds with the addition

and/or release of chemical groups

Isomerases- Catalyze the rearrangement of chemical groups in a substrate

Transferases- Catalyze the transfer of chemical groups from one substrate to

another

Of these six categories, we are most concerned in this information sheet with

the first two i.e., the hydrolases and the oxioreductases. These two categories

are most often used clinically as food supplements. The hydrolases include

proteases that catalyze the digestion of proteins, amylases that catalyze the

digestion of sugars and starches, and lipases that catalyze the digestion of

fats.

The digestive properties of hydrolase enzymes make them a multi-faceted tool for

clinical use. Their activity is not limited to the simple digestion of food but

extends systemically. Studies on proteolytic enzymes have shown them to have

excellent anti-inflammatory and micro-circulatory enhancement properties

(Pizzorno and Murray, pp. 857-869, Wolf and Ransburger, pp.84-100). These

properties are attributed to the fibrinolytic and thrombolytic activities of

certain hydrolases. The anti-inflammatory mechanism of proteolytic enzymes is

different from prescription anti-inflammatory drugs (steroids and non-steroids).

Unlike drug therapies that seek to suppress natural damage response mechanism,

supplemental enzymes are very similar to the enzymes found in the body. They

enhance the body’s natural damage repair mechanisms and controls so there are no

adverse side effects to restrict the time of therapeutic use.

Inflammation is a highly complex process that is the result of cellular assault

from one or more sources including chemical, physical and biological.

Inflammatory conditions are known by many names. Allergy, arthritis, sunburn and

other burns, sprains, strains and other athletic and soft tissue injuries,

pancreatitis, hepatitis and many other ‘–osis’ and ‘–itis’ conditions are

included in the list. Many conditions that have their origins in the

inflammatory process do not come to mind as readily as some of those listed

above. These include arteriosclerosis, atherosclerosis, adhesions and scarring.

Many of the conditions listed above have similar biochemistry (Crouch and

McClintic, pp.461-464, Pizzorno and Murray, p. 863, Wolf and Ransburger, pp.

34-68). Once damage is done to the cells biochemical changes occur which change

the permeability of the cell membranes and the surrounding capillaries leading

to the formation of exudates. Swellings, redness, pain and sometimes fever

follow. Leukocytes and macrophages concentrate at the site and begin to digest

the damaged and dying cells (phagocytosis). Phagocytosis by mature leukocytes is

accompanied by a rapid uptake of oxygen by the phagocytes and the appearance of

the superoxide radical in the area around the damage site, possibly as an

anti-infection response. The superoxide radical is highly toxic to many foreign

bacteria (Montgomery, Dryer, et al, pg. 219). Fibrin forms as fibrinogen is

exposed to the destroyed and damaged tissue and the specialized proteins

released by the damaged cells. This is the beginning of the clotting process and

serves to lock-up or ’fixate’ toxins at the site to minimize damage to

surrounding tissue. The clotting leads to a reduction of blood flow to the

damaged region resulting in edema and pain. As part of the body’s repair process

proteolytic enzymes, most notably plasmin, are sent to the injury site to begin

the process of exudate removal and fibrin breakdown, even as the fibrin forming

process is just beginning. This accounts for studies showing that proteolytic

enzyme supplementation immediately after an injury (or prophylactically) results

in a significant reduction in both the severity and duration of inflammation

(Wolf and Ransburger, pp. 84-92). Commonly, especially in older victims, excess

fibrin formation occurs leading to an exaggeration of inflammation symptoms and

an increased risk of necrosis and scar formation. Thus, the importance of

systemic enzymes like plasmin and others serve as part of a regulatory mechanism

which inhibit the effects of cellular damage on surrounding tissue becomes

obvious.

Through the processes of stress, aging, poor nutrition and other factors,

including severity of injury, the body’s natural anti-inflammatory enzyme system

often operates at a substantially reduced level leading to long term

inflammation and resultant pain, edema and thrombi. Supplemental enzymes can be

of great assistance in controlling the problems associated with inflammatory

processes.

Plasmin-like enzymes commonly used in enzyme supplementation include trypsin,

a-chymotrypsin and pepsin. The activity of these enzymes, like that of plasmin,

involves cleaving polypeptide chains, usually at particular types of amino acids

with differing degrees of specificity. Their great activity is due to the

property of cleaving proteins at sites inside the polypeptide chains

(endopeptidases), not just at the terminal end. They also work together to

solubilize large proteins into short non-coaguable polypeptide chains. Other

supplemental enzymes include papain, a phytoenzyme that has a less specific but

potent proteolytic activity and bromelain, also a phytoenzyme, which is a potent

proteolytic enzyme and has been shown to activate plasmin from plasminogen, a

proenzyme. Pancreatin is an extract of pancreas containing a mixture of several

proteolytic, lipolytic and amylytic enzymes. Lipolytic enzymes like lipase and

pancrelipase are important in solubilizing fats to fatty acids and glycerol.

Amylitic enzymes like amylase split starches into saccharides and smaller

polysaccharides.

An important adjunct enzyme system in the body’s damage repair mechanism

includes the oxioreductase enzymes superoxide dismutase (SOD) and catalase.

These two enzymes work as a team to reduce the highly destructive superoxide

radical (O2-) to two H2O molecules via hydrogen peroxide (H2O2). The superoxide

radical is often sited as one of the main culprits in premature aging and

reduction in cell growth rates (Pizzorno and Murray, pp. 831, Stipanuk, pp. 757,

907, Wolf and Ransburger, p. 114). The superoxide radical is certainly

responsible for cell wall damage and the presence of SOD and other oxioreductase

enzymes and coenzymes are necessary to prevent adjacent cell damage. A defect in

SOD has been implicated in a form of Amyotrophic Lateral Sclerosis. (Blaylock,

p. 122) Glutathione is an important electron-transfer link in this repair

mechanism as well as enabling amino acid transport across cell membranes.

Glutathione is essential in maintaining sulfhydryl bonds in the reduced state in

a variety of tissues and is a potent enzyme activator.

To cut costs, some manufacturers claim that their enzymes contain glutathione

because they add the three constituent amino acids, L-glutamic acid, L-cystein

and L-glycine to their product. This assertion is false. Glutathione is a

tripeptide. There is no indication that the three free-form amino acids that

make up glutathione will be used to manufacture it in the body if supplied in

this manner. Similarly, some manufacturers claim some of their trypsin activity

as a-chymotrypsin, a critical but expensive peptidase, without actually adding

much, or, sometimes, any. If you are not sure, ask the manufacturer if they are

actually using glutathione and a-chymotrypsin.

There are other important aids to oxioreductase enzymes besides glutathione and

catalase. One of the most important is a-lipoic acid. This molecule attaches to

enzyme-substrate complexes. It acts as a coenzyme in the transfer of electrons

and activated acyl groups from one substrate to another. The physical structure

of the molecule is such that it can " swing " around in an arc and its’ disulfide

bond can be reduced for the electron transfer. Several of these molecules often

line up and act as a shuttle to perform their transfer functions (Zubay, pp.

369-371). a-Lipoic acid doesn’t just reduce the superoxide radical. It also

reduces the hydroxyl radical, hypochlorous acid and oxygen singlets and chelates

free copper and iron. a-Lipoic acid also has the ability to regenerate other

free radical scavengers like vitamins C and E as well as SOD and catalase from

their oxidized state (Blaylock, pp.245-248). Thus, an SOD-lipoic acid-catalase

complex is highly important in preventing damage to cell walls and protects DNA

from damage from free radicals.

Lyophilized calf thymus is included in Megazyme and Megazyme Forte because,

according to researchers, lyophilized thymus is rich in nuclease enzymes.

Nucleases are hydrolases, which cleave the phosphodiester bonds of DNA and RNA.

Damaged and foreign RNA/DNA are readily digested by these enzymes. Thus, a viral

invader is susceptible to the two-pronged attack of proteases on its’ protein

coat and nucleases on its’ genetic material (Wolf and Ransburger, pp.119-133).

One of the major problems of enzyme supplementation is getting enzymes that are

pH sensitive past the stomach to the duodenum where absorption takes place. In a

supplement designed to enhance digestion, this can be accomplished by using a

two-phase strategy. Pepsin is in its most active state at very low pH and papain

is active in a very wide pH range. Therefore, no special protection is required

for these two enzymes. They are quite active in the stomach. On the other hand

trypsin, a-chymotrypsin, pancreatin, SOD, amylase, lipase, catalase, glutathione

and other activators, enzymes and coenzymes are susceptible to deactivation or

destruction by stomach acids. A method must be devised to protect them through

the stomach but make them available for absorption in the duodenum. This is the

reason these types of products cannot be made in capsule form. Instead, we use

tablets with a special coating to protect the contents and release them at the

proper time. In the case of Hypo Gestaid, Mega Gestaid and Chelaplex a special

coating and tablet pressing technique is used to provide the two-phase tablet

mentioned earlier. Megazyme, Megazyme Forte and SOD/Lipoic Acid Complex are

specially coated for protection from the highly acidic conditions of the stomach

and maximized absorption and activity at the proper sites.

Rocky Fork Formulas currently carries five products that use hydrolase enzymes

as their main ingredients. These are the two-phase digestive aids Hypo Gestaid

and Mega Gestaid, the specialty enzyme mixtures Megazyme and Megazyme Forte and

the oral chelation supplement Chelaplex. Chelaplex, Megazyme and Megazyme Forte

also contain oxioreductase enzymes. The ingredients of these enzymes products

are listed below.

Mark E. Armstrong

www.top5plus5.com

Oregon State Chapter Rep

Pancreatitis Association, International