One of the functions of the digestive tract is to change food into a substance that won’t trigger the immune system to launch an attack.

Several methods are used in the body to accomplish this task.   Stomach acid denatures food proteins.  Denaturation removes the “glue” holding the structure of the food protein together and often results in loss of any function associated with the protein.

However, even denatured proteins can be allergenic.   The next and most definitive step for rendering food proteins harmless is enzymatic degradation that begins in the stomach but predominates in the small intestine.  Denaturation actually sets up the protein for optimal break down by protease enzymes.

The immune system in the gut is triggered by a number of factors but size of the offending protein is the most predominant.  The larger the protein, the more likely it is to set off the alarm for IgG antibody production.  Conversely, smaller proteins or fragments are able to slip under the radar for immunity activation.  Research from several labs demonstrate that when protein digestion is compromised, antibody production to that food protein increases (1 – 3).

A compromised digestive system can occur easier than one may think.

The simple act of taking an antacid reduces the activity of pepsin, the major protease enzyme in the stomach, by raising the pH of the stomach over 5.0.  Many on H2-receptor blockers have increased food allergy symptoms because the resulting low stomach acid fails to activate the pepsin enzyme system.

Larger food protein fragments are then passed on to the intestinal tract and have the potential to become allergens (2 – 4).  Conversely, research indicates that pre-treatment of food proteins with protease enzymes results in a less allergenic potential (5 – 6).  Heating of a protein alone will not break down a food protein sufficiently, so cooking is no guarantee of allergy prevention.

The World Health Organization proposed in 2001 that food proteins be tested for the allergenic potential.  One of the parameters for consideration is the resistance to enzymatic digestion by some food proteins (7).  A positive association was found between resistance to digestion and development of food allergy.  Food proteins with a high content of proline amino acids, like gluten, are very difficult to digest by human digestive enzymes.

What does this mean for the consumer?  Obviously, increasing the digestion of food proteins decreases the chances of potential allergy development.  Unfortunately, our own digestive enzymes are not always sufficient.

By supplementing with additional acid-stable enzymes from plant sources we can increase the chance of food proteins being sufficiently degraded.

These “outside” sourced enzymes are compatible with our digestive systems but have additional properties that provide us with more thorough digestion.  The use of supplemental enzymes increases the bioavailability of food nutrients to our system, provides a healthier environment for the probiotic bacteria in our gut, and eliminates the unwelcome side effects of unhealthy digestion, such as fermentation, gas, and bloating.

Oral tolerance of food proteins is an important aspect of our digestive and immune system.  The use of over-the-counter enzyme supplements specifically formulated for protein digestion (such as AFP-Peptizyde from Houston Enzymes) may further increase digestion of food proteins. Broader spectrum enzyme products, such as TriEnza from Houston Enzymes, benefit not only protein digestion, but breakdown of carbohydrates, starches, and fats is also increased.

References:

1. Anthoni S, Savilahti E, et al. Milk protein IgG and IgA: The association with milk-induced gastrointestinal symptoms in adults. World J Gastroenterol 2009; 15:4915-4918.

2. Schmidt DG, Meijer RJ, et al. Raising the pH of the pepsin-catalyzed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates. Clin Exp Allergy 1995; 25(10):1007-17.

3. Untersmayr E, Scholl I, et al. Antacid medication inhibits digestion of dietary proteins and causes food allergy: a fish allergy model in BALB/c mice. J Allergy Clin Immunol 2003; 112(3):616-23.

4. Untersmayr E and Jensen-Jarolim, E. The role of protein digestibility and antacids on food allergy outcomes. J Allergy Clin Immunol 2008; 121(6):1301-10.

5. Kim SB, Ki KS, et al. Peptic and tryptic hydrolysis of native and heated whey protein to reduce its antigenicity. J Dairy Sci 2007; 90(9):4043-50.

6. Burks AW, Williams LW, et al. Allergenicity of peanut and soybean extracts altered by chemical or thermal denaturation in patients with atopic dermatitis and positive food challenges. J. Allergy Clin Immunol 1992; 90(6 Pt 1):889-97.

7. Bannon G, Fu T-J, et al. Protein digestibility and relevance to allergenicity. Environ Health Perspect 2003; 111:1122-24.

Note: These statements and/or products have not been evaluated by the FDA and are not meant to diagnose, cure, treat, or prevent any illness. Please consult your medical doctor for treatment options.

866-757-8627 info@houston-enzymes.com

Copyright © Houston Enzymes 2011.

A new study published in the journal Neuropeptides appeared to implicate low levels of DPP IV, an enzyme found in the gut and other tissues, with onset of Sudden Infant Death Syndrome.  DPP IV breaks down certain peptides known as exorphins that have opiate-like properties.  Exorphins are similar to endorphins except that exorphins are derived from food sources.  This latest study found levels of casomorphin, an exorphin derived from casein, to be much higher in the blood of infants who had had near-SIDS episodes.  These same babies also had low levels of DPP IV.

This study was very small and very preliminary.  Parents should not be overly concerned about feeding babies formula.  As the study mentions, there are much greater risks that promote SIDS than casomorphin.  I do find it interesting on several points: 1) it indicated that casomorphin could escape from the guts of these children, even though no sign of inflammation or “leaky gut” was present.  2) The study failed to mention the potential sources of other exorphin peptide, such as wheat and soy.  Many parents use soy-based formulas as an alternative to dairy-based, but soy protein can produce soymorphins.  3) The nervous system of infants is not fully developed.  Neither is the blood-brain barrier which is designed to limit the passing of proteins, peptides and other compounds from the blood into the brain.  4) It is further evidence of the power of food in producing bioactive peptides.   Their effect should be seriously considered in other disorders, such as autism and ADHD.

Should all parents now rush out and have their children tested for levels of DPP IV? I think not.  Should we examine what is in the formulas given to infants? I would think so.  Should moms consider breast-feeding longer?  Definitely, but that is a personal choice and no undue pressure should be exerted one way or the other.  My advice is to be aware and trust those maternal instincts.

Reference: The exogenous opioid peptides and DPPIV serum activity in infants with apnoea expressed as apparent life threatening events (ALTE) –  Jolanta Wasilewska, Edyta Sienkiewicz-Szłapka, Ewa Kuźbida, Beata Jarmołowska, Maciej Kaczmarski and Elżbieta Kostyra

Whatever the results, secretin is not an enzyme, it is a hormone that causes the pancreas to release enzymes into the gut.  Secretin is quite different from enzyme supplements, which do not require any action by secretin to start breaking down foods and enhancing digestion.  http://usat.ly/hoTzUS

We started with Peptizyde and HN-Zyme Prime and sold our first product in April of 2001.  It is hard to believe how far we have come since those days, and how quickly the years passed.

Every year of business has been better than the previous and we take that as a vote of confidence by our customers.  We took a unique product that addressed a definite need and asked for your trust in using it.

The feedback was outstanding and humbling to me.  My biggest blessing over the years is the many stories told of children getting better and families leading more normal lives.  I love meeting you and your kid at the conferences, the hugs from the moms, and seeing the smiles on your child’s face.

Top Ten (Year) Reasons to Use Houston Enzymes

#10.  Fast, flexible ordering online or by phone. In most cases, your order is shipped out the day you order.  Call our toll-free number and talk to one of our Customer Service representatives if you have a special circumstance that needs addressing.  You can leave your order on our secure voice-mail any time of the day or night.  Our website,www.houston-enzymes.com, also allows 24/7 ordering.

#9.  Customer access to the product formulator/company owner. Many CEOs insulate themselves from customers, delegating customer questions to employees.  As the company owner and product formulator, I try to make myself available to answer questions that need specialized attention.  You can reach me by email, phone, Facebook, orTwitter.  I do my best to answer questions by the next business day.

#8.  Digestive results may be observed quickly. I formulate my products with high amounts of enzymes in order that you may achieve quick results to your digestive problems.  In most cases, a noticeable improvement may be realized within the first 3 days of enzyme use.

#7.  Completely plant-based enzyme products. My enzyme formulations use only plant-based enzymes.  No pancreatic enzymes derived from animal sources are used.  Even the capsule is plant-based.

#6.  Unique product line allows for customized enzyme use. Our products are designed to focus on specific dietary food issues.  We don’t believe in “one product fits all” formulations because your diet and digestion can vary from others.  Our products are designed to be “mixed and matched” to your specific dietary needs.

#5.  Safety. Great care has been taken to provide our customers with the most potent and safe products available.  We use a manufacturer with top-rated laboratory and Quality Control protocols in place. Enzymes are one of the safest supplements in the industry.  No chance of over-dosing since there is no toxic limit for any digestive enzyme. Enzymes will not interfere with most medications or other supplements. Our only caution is that enzymes are protein and therefore have the potential to be allergenic, though this is rare.  If you have never used an enzyme product, use caution until you are sure you are not allergic to enzymes.

#4.  Increases bio-availability of food nutrients. Oral enzyme supplements increase digestion of foods.  If foods are more thoroughly digested, then the minerals, vitamins and other nutrients will be made available for absorption in the GI tract.  Oral enzymes act to support normal digestion.

#3.  Provides for a more healthy gut environment. Any undigested foods within the gut can be a source of growth for bad bacteria and yeast.  By ensuring that foods are broken down completely in the gut, less likelihood exists for bacterial blooms.

#2.  Houston Enzymes products can be an alternative to some restrictive diets. Many food intolerances can be diminished or eliminated by the proper use of proteolytic and carbohydrase enzymes. Our enzyme products are acid-stable and work in the stomach (where proteins and peptides are NOT absorbed).  This allows problem foods to be broken down in the “safe house” of the stomach.  By the time the food mass enters the small intestine, those foods are no longer a source of intolerance.  Because of this attribute, our enzymes can be used with diets or as a substitute to certain diets.  This allows a little more freedom and flexibility in the planning of meals and family nights out.

And the Top Reason to use Houston Enzymes:

#1.  Houston Enzyme products are formulated by an enzyme biochemist. Let’s face it.  There are many enzyme companies out there claiming to be enzyme “experts”.  But you be the judge.  Would you rather your enzyme products be formulated by someone with an earned doctorate in Medical Biochemistry, demonstrated ability and publications in the area of enzyme biochemistry, and industrial experience in enzyme dietary supplements?  That is what you get when you use products from Houston Enzymes.

It’s easy to say you’re an expert when no one asks you to prove it, so go ahead, ask us!  Then ask the other companies…  

- Devin Houston

Americans continue to be fascinated by the whole issue of stomach acid.  From “Plop, plop, fizz, fizz, oh what a relief it is,” to the irritating commercials on acid reflux, we always seem to be unhappy with our acid situation.

HCl is secreted by special cells in the stomach wall.  There is always some amount of acid being produced, but acid really pours out when food enters the stomach.  The HCl does not break food down; that is left up to the enzymes. 

Acid does prepare foods for digestion, especially proteins.  Normally, proteins exist in a tightly coiled globular structure.  Acid denatures the protein which results in the protein unraveling into a more linear structure.  This then allows enzymes access to the peptide bonds so the protein can be broken down.

Acid also jump-starts enzyme activity.  Above pH 5.0, stomach enzymes are inactive.  Once acid lowers the pH to under 5.0, they become active.  This is why those on acid-reflux meds often get relief from the reflux but their digestion becomes less than optimal.  The lack of acid prevents our own enzymes from working.

Luckily, enzyme supplements do not need HCl to be active because they are already in an active form, once they are in solution.  Our plant-based enzymes can function in a broad range of pH, usually from 2 to 9.

I am often asked if I recommend taking betaine HCl.  If one takes enzyme supplements I really see no need for doing so, but it also won’t hurt the enzymes either. 

If you feel better taking the betaine, then by all means use it.  Your Houston Enzyme supplements will work just as well with or without it.

Over the past year, reports have surfaced indicating that gray hair may be caused by an accumulation of hydrogen peroxide in hair shafts.  This appears to be a result caused by deficiencies in certain metabolic enzymes such as catalase, methionine sulfoxide reductase, and tyrosinase.

It didn’t take long for some dietary supplement companies to take this information and provide a so-called “solution” to the problem. 

Some products have popped up espousing the use of catalase, an enzyme involved in the breakdown of hydrogen peroxide and other free radicals, in an oral supplement to reverse the graying of hair.  Playing on the vanity of those who can’t accept that they are getting older (and showing it) is a sure-fire way to make a buck these days.

Unfortunately, these products don’t work because catalase is an unstable enzyme easily degraded by stomach conditions.  Even if it did survive the gut, there is no way to direct the catalase specifically to hair follicles - it would simply be distributed throughout the circulation and then removed by the body’s defenses.

I am a guy in his fifties whose hair is full of gray.  I actually get a lot of compliments on my salt-and-pepper look, and I know I wouldn’t be fooling anyone if my hair suddenly became dark again.

This myth states that taking enzyme supplements is a waste of time and money because the enzymes, being proteins, are denatured (destroyed) by the acid in the stomach.

I actually once believed this statement because it was taught to me in medical school.  Not til I was challenged to verify the statement did I find that what I was taught was not completely true.  The majority of enzymes, including pancreatic enzymes, are not stable under acid conditions and so are not effective taken orally.  There are two exceptions: enzymes that have been enteric-coated (that is, treated with a substance that prevents contact with stomach acid) and PLANT-BASED ENZYMES.  The problem with enteric-coated enzymes is that the coating prevents enzymes from working in the stomach.  Only in the neutral pH of the small intestine will they finally function.  Plant-based enzymes, which comprise the bulk of enzyme supplements, are derived from plant organisms that secrete acid-stable enzymes.  These enzymes have been purified and characterized so their pH optimum (acidity/alkalinity at which they work best) is well known and easily determined.  The majority of these enzymes can work in a pH range of 2 to 9 with no loss of activity.  This is not an opinion.  The enzymes can be assayed under lab conditions at different pH and this is easily verified by enzyme manufacturers.

The ability of enzymes to work in the stomach provides the means by which protease enzymes degrade gluten, casein, soy and other food proteins.  The peptides that many find intolerable are degraded or not produced.  The stomach actually becomes a "safe house" when a child that does not tolerate dairy ingests these foods.  No peptide or protein absorption occurs in the stomach, so one has a couple of hours to use the enzymes to break down the proteins before they move into the small intestine where the bulk of protein/peptide absorption will occur.

I was humbled years ago when I had to come back and admit to my "challenger" that I was mis-informed about plant enzymes and their acid stability.  It taught me not to take a teacher’s word, but to verify the subject matter for myself.  I highly recommend others do the same.

Ah, the magical 118 number! When Edward Howell wrote his book on enzymes, he concluded that at above 118 degrees Fahrenheit, all enzyme activity would cease. Remember, this was someone who wrote the bulk of his material between 1930 and 1950. Determining enzyme activity and temperature profiles was not a precise science back then.

Actually, most plant-based enzymes are extremely hardy in regards to enduring high temps. Papain is probably the champ, as it is able to withstand temperatures as high as 190 degrees F for several minutes without being denatured. Most of the enzymes used in supplements are assayed for activity at temps ranging from 110 to 140 F. Enzyme assays are usually performed under conditions considered optimal for maximum activity, so obviously these temps are nowhere near the danger zone for these hardy proteins.

The notion that one temperature (118 F in this case) applies to all enzymes as the point of thermal inactivation is also not true. Resistance to heat varies with every protein, some are extremely sensitive, others are not. All plant-derived enzymes should be able to accommodate temps of 125 F with no problem.

Let’s put the above information to practical use. Summer temperatures are often a concern to customers when it comes to shipping enzymes. However, this is not a problem as the packaging and bottle should provide adequate shielding from direct heating. The worse scenario would be a package of enzymes left in a hot metal mailbox, but even this would have little effect on the enzyme activity.

Since we are discussing temperature: The best way to prolong the shelf life of your enzymes is to keep it in the bottle in the freezer. Don’t put it in the refrigerator for prolonged periods. Refrigerators have high humidity levels, freezers do not. Humidity is the worst enemy of enzyme activity, so take care to keep them in a dry place. Enzymes love the cold, so the colder the better. This is especially helpful for the chewable tablets as it keeps the tablets from getting soft (though this has no effect on the activity) which sometimes occur if a bottle is not completely emptied in a month or so.

Another comment bears repeating, though it may seem obvious. Don’t cook the enzymes. Wait until any cooked food has cooled before adding or mixing enzymes. The rule of thumb is if it’s cool enough to put into your mouth, it’s cool enough to add enzymes.

Just remember: Enzymes are cool!

Now that’s interesting. Enzymes are proteins, and any protein, even an enzyme, will eventually be broken down by the body’s own set of protease enzymes. No protein taken orally will survive intact for long (though plant enzymes are more resistant), even those that do get absorbed into the circulation. Our bodies would much rather use ingested proteins as raw materials to build its own proteins, when and where they are needed.

Another question: How would one know that the ingested enzyme is being stored? And why in the liver? And how would the liver know when we "needed" the enzyme? The liver is an organ of detoxification and produces many of its own enzymes to metabolize drugs and remove toxins (which is why I don’t eat livers, yuck!). It does not store anything.

But yet I keep seeing that statement on this company’s website, and it annoys me. They should know better. It could be that they subscribe to the unproven and debunked theory of enzyme conservation and mutation, whereby it is thought that a deficiency of enzymes in one part of the body can result in the recruitment of other enzymes in the body to compensate. But that is another myth to be scorned upon at a later date.

Bottom line: Enzymes taken orally do NOT get stored anywhere in the body. The vast bulk of the enzyme will remain in the gut, loyally accompanying and breaking down the food it was eaten with until it is inactivated or pooped out. And this is a good thing, we would not want the enzymes we eat, which are in active form, to be stored as they are foreign to the cells of our organs . In other words, the organs would not know what to do with the enzymes except tear them up or activate the immune system and remove them which is what eventually happens to any ingested enzyme/protein absorbed into the circulation.

More debunking to come…

It was during those vacations we first encountered fireflies: those magical flying lanterns! Ever the scientist, even at 14, I was fascinated that a small insect could produce light. How could it do that and not get hot like a light bulb?

Fast forward to 1981. I’m a graduate student at the University of South Alabama College of Medicine and starting work on a doctoral thesis. One of the first things I learn is how to determine the activity of an enzyme known as phosphodiesterase or PDE. The assay used an extract of firefly lanterns (containing luciferin and the enzyme luciferase) to produce a small amount of light that was then measured with a luminometer. Combining the luciferin-luciferase extract with ATP (the energy source for many cellular functions) and the PDE enzyme resulted in obtaining PDE activity by measuring the amount of light produced from the firefly lantern extract. On a historical note, the extract was obtained from Sigma Chemical company in Saint Louis, MO. It was one of the first products made by the company back in the 1940′s. People, including children, were paid to collect the fireflies from Forest Park near the Central West End of Saint Louis. Even today, Sigma will pay about a penny per firefly!

As a child I didn’t imagine ever finding out how fireflies worked. As an adult, I sit on my deck in the summer evenings and watch the flying lights.

I know how they light up now.

But the wonder remains.