Make Sure Digestive Enzymes Don't Contain FungusIdeally, you should get your digestive enzymes from your food (raw foods, fermented foods, homemade yoghurt, etc) and from your body’s own production.

However, for those times when you just cannot get enough natural enzymes, or you need some additional support as your own body’s production is not up to par. I have found these high quality, natural enzymes in both a capsule and chewable form that you can eat with or after meals.

Many digestive enzymes are cultured on aspergillus oryzae (mold). But then are not filtered properly, and you end up ingesting the spores – not good for someone with unbalanced or susceptible gut flora to begin with!

This is the main reason I stayed away from using or recommending digestive enzymes for so long.

But, thankfully, filtration technology has improved. And these Houston TriEnza Enzymes (derived from Aspergillus) have been purified from the fungal matter using 8 to 12 different methods of purification. Meaning there is NO fungal matter present in this enzyme product! 

If you have a known allergy to Aspergillus proteins, then caution should be used in taking any fungal-derived enzyme product, however, the allergenic portions of Aspergillus are usually those parts of the fungi removed from the enzymes during processing.

The other reason I like this particular brand is they combine ALL the enzymes needed – for protein, carbohydrate and fat digestion – into one product. They do not contain cellulase though, so they won’t interfere with timed-release medication.

When To Take Enzymes

Take digestive enzymes with the first few bites of your meal or just prior to mealtime. But more important is to take the enzyme, if not at the beginning, then during or after eating. Food stays in the stomach for up to 3 hours. Therefore, introducing enzymes anytime during the meal will still provide benefits.

If you’re a “grazer” who eats constantly during the day. You may wish to take the enzymes at fixed dosing intervals, such as every 4 or 5 hours during the day.

*Note: Remember, that if you’re having more than 3 bowel movements per day, you must not swallow pills/capsules (gut transit time is too fast) – in that case, it would be best to use the chewables.

What Are Enzymes?

Enzymes are proteins made by cells in our bodies. They are specialized proteins that do work. Such as synthesizing chemicals and compounds, rearranging molecules, adding elements to compounds, and breaking down compounds.

There are many types of enzymes, and each type does a specific function. For an enzyme to work, it must have access to its substrate, the material upon which an enzyme exerts an action. If no substrate is available to the enzyme, the enzyme performs no function. For example, an enzyme called catalase is present in our blood.

Catalase converts hydrogen peroxide to water and oxygen. This is why there are peroxide bubbles when it is placed on a wound.

Since peroxide is not usually in our blood, catalase circulates within the blood, doing nothing until peroxide is introduced into the system. A substrate works as an “on-off” switch for its particular enzyme. Catalase will only be activated in the presence of peroxide and nothing else.

How Do Enzymes Work?

Enzymes work as catalysts of biochemical reactions. A catalyst increases or accelerates the rate of a chemical reaction. The thousands of chemical reactions that occur in our body every second could not happen without enzymes to speed up these reactions. For example, a protein can be broken down into amino acids in the lab without the use of an enzyme. But to do so requires extreme temperatures, high pressure, and very strong acids; conditions not compatible with life.

Even with these conditions, it requires hours to complete the reaction in the lab. With enzymes, in this case a mixture of proteases, the reaction can be completed within minutes in water at normal temperatures.

enzymesAnother unique aspect of enzymes is that they are not changed during the reaction, that is, they facilitate the reaction without being destroyed or changed in the process. Because of this, one enzyme molecule could theoretically change an infinite amount of substrate. If given an infinite amount of time.

Increasing the amount of enzyme decreases the time required for completing the reaction. For example, one molecule of catalase could convert a whole bottle of peroxide to water and oxygen given enough time.

If you double the number of catalase molecules, you decrease the time for converting the bottle of peroxide by half.

This is related to enzyme dosing in the following manner:

Higher doses of enzyme will result in the reaction reaching the “finish point” faster. Since a meal resides in the stomach from 90 to 180 minutes, the enzymes have that amount of time to do the majority of their work before the food enters the small intestine. There peptides may be absorbed (no peptide absorption occurs in the stomach).

Larger meals will require more enzyme to accomplish the task of food breakdown in a given amount of time. This is the applicable message concerning enzyme dosing; getting the proteins broken down in a specified period of time.

The nice thing about enzymes is that if the particular molecule they work on is not present, the enzyme does nothing. If you take the enzyme lactase, and lactose is not present, the lactase has no job and does nothing, except get passed on in the GI tract as food protein.


Original post dated May 2011. Most recently updated October 2023.