Enzyme Sources

Since the late 19th century scientists have been studying animal enzyme sources. Their focus was on cancerous tumors and the effect of enzymes on them. This was because cancer cells are surrounded by protein to protect them from the immune system. They studied how trypsin, chymotrypsin and pancreatin break down protein to expose the cancer cells to the immune system. Other areas of study with enzymes include heart disease, and stroke and inflammation. Fibrin, which is a protein, contributes to these diseases by causing blood clots. Protease breaks down the fibrin and can reduce inflammation. Most people don’t know that inflammation can cause a heart attack.

Pigs and cows were slaughtered and the enzymes were extracted from their pancreases. This was the only source of enzymes about fifty years ago.

What are the disadvantages of animal source enzymes?

If you were a vegetarian you would not want to consume them. Also, animals can be exposed to antibiotics and steroids, which wouldn’t be healthy. Thirdly, they’re weak compared to microbial enzymes. Animal enzymes are unstable at a low pH or acidic environment. Since the stomach is acidic much of the enzyme is destroyed before it can do its job. One way to get around this would be to put the enzymes in an enteric-coated tablet. This coating doesn’t dissolve in acid. Thus it dissolves in the intestine, which isn’t acidic. One popular brand that’s enteric-coated is Wobenzym N.

They are also temperature sensitive and since we don’t have the same body temperature as the animal source this can affect the enzyme.

What are the advantages of animal source enzymes?

The advantage is what is called the law of similar. The law of similar is the basis of homeopathy. The theory is although the source is not human your body recognizes it as similar and therefore is able to use it more effectively.

The two types of plant-based enzymes are bromelain, which comes from pineapples and papain, which comes from papayas. They are quite stable in acidic pH and are not affected by temperature. One disadvantage is they are only beneficial as digestive enzymes. They can’t be used as systemic enzymes. Another is they could contain harmful substances such as phenolic compounds.

Most enzyme sources come from fungi or yeast. Some consider this plant-based but fungi are actually not plants. This is because the study of fungi has historically been a branch of botany. The most popular fungus used is called aspergillus. Over half of enzymes come from fungi and yeast, over a third from bacteria. About 8% are from animal sources and 4% from plant sources.

What are the advantages of microbial enzymes?

They are usually cheaper to produce. They are extracted from fermented fungus or bacteria. Their enzyme contents are more controllable and predictable. Manufacturers can manipulate aspergillus fungus in order to make different types of enzymes. This is done by changing the type of aspergillus that’s used. They’re the most potent enzymes and can be up to a hundred times more effective digesting proteins, carbohydrates and fats. One doesn’t have to worry about contamination with antibiotics or steroids. The pH range is broad which makes them active in stomach acid and throughout our body. Last but not least, there is a reliable supply of raw material to make microbial enzymes.


Catalase Liver
Lipase Pancreas


Actinidin Kiwi Fruit
Ficin Fig Latex
Lipoxygenase Soybeans
Papain Pawpaw Latex


a-Amylase Aspergillus
Catalase Aspergillus
Dextranase Penicillium
Glucose Oxidase Aspergillus
Lactase Rhizopus
Pectinase Aspergillus
Pectin Lyase Aspergillus
Protease Aspergillus
Raffinase Mortierella


Invertase Saccharomyces
Lactase Kluyveromyces
Lipase Candida
Raffinase Saccharomyces