The question, What Are Enzymes, is an important one. Did you know that enzymes rule every single system in your body—as well as all of their parts? Your immune system, digestive system, blood, liver, kidneys, spleen, and pancreas—as well as your capability to see, think, breathe, and feel–the functioning of every cell in your body—are all contingent on enzymes. All of the minerals and vitamins you consume and all of the hormones your body produces must have sufficient enzymes to work correctly. Your stamina, your energy level, your ability to utilize vitamins and minerals are all governed by enzymes.
What are Enzymes?
An oversimplified explanation of nutritional enzymes is that they are catalysts – proteins that speed up chemical reactions. That is, they cause other reactions to occur in the body, or they aid in certain metabolic processes. Enzymes play a vital role in everyday life. In fact, they regulate every single part of your body, including all of your tissues, muscles, bones, organs, and cells.
A nutritional enzyme (an enzyme found in dietary supplements or the body) is a very specific type of protein. In the case of protein-digesting (proteolytic) enzymes, they are proteins that break down other proteins. Any unused ingested enzymes are simply converted into amino acids and utilized by the body differently. Amino acids are what the human body converts protein-based foods into for nutrition, which is why proteolytic or pancreatic enzymes are some of the safest compounds to ingest even in substantial quantities if needed.
Estimates suggest that between 55,000 and 75,000 (the majority have not been identified) different enzymes in your body regulate every metabolic function in your body. Without enzymes, all of these metabolic functions would progress through the same steps but would go too slowly to sustain life. In essence, enzymes make life happen where otherwise there would be none.
Most of the time, we think of enzymes as being digestive enzymes. However, there are tens of thousands of different enzymes in the human body, and 99.999% have nothing to do with digestion.
How You Take Enzymes Is Important
A fundamental concept to understand is that digestive enzymes formulas and systemic/metabolic, proteolytic enzymes formulas are not always the same thing even though they may share many of the same enzymes. For instance, when you take a digestive enzyme formula with your meal, the enzymes work on speeding up the breakdown of the food in your stomach. I like to think of them as little pac-men quickly going around and breaking down food. On the other hand, when you take a proteolytic enzyme formula between meals, the enzymes do not get stuck working in your stomach or wrapped up with your food and passed out through the colon. Instead, they quickly enter your bloodstream. Once in the bloodstream, they help optimize your blood, plus they make their way to all of the tissues throughout your body, where they assist with intelligent, adaptive healing.
Let’s discuss the different types of enzyme groups and what they do in the body.
Types of Enzymes
PANCREATIC ENZYMES
Enzymes that are delivered to the duodenum by the pancreas during the digestive process would be our own naturally produced pancreatic enzymes or a nutritional supplement containing pancreatic enzymes derived from animal pancreas. The most common pancreatic enzymes are Pancreatin, Trypsin, Alpha Chymotrypsin (also known as a-chymotrypsin), Lipase, and Amylase. There are others, but these are the most common. The enzymes Trypsin and a-Chymotrypsin are potent protein-digesting enzymes. The enzyme Amylase digests starch, and the enzyme Lipase digests fat. The enzyme Pancreatin is not a specific enzyme but is an enzyme slurry that contains all of the previously mentioned pancreatic enzymes.
PROTEASE AND PROPRIETARY BLENDS
There is no such enzyme as “protease.” Protease merely refers to ANY enzyme that digests protein. The category of protease can include any of the protein-digesting pancreatic enzymes as well as any of the protein-digesting vegetable, fruit, or other based enzymes. Some enzyme formulas display their contents in a “proprietary blend” of protease that displays an impressive list of enzymes containing Trypsin, Chymotrypsin, and other potent pancreatic enzymes as well as some vegetable enzymes like Bromelain and Papain. Quite often, the term “proprietary blend” is just a smokescreen to hide the fact that some are using minimal amounts of highly active enzymes and large amounts of lesser active enzymes. The concern here is that you just don’t know how much of each enzyme is in the Proprietary blend. A “proprietary blend” only tells you what enzymes are in the mixture and conceals the actual potency of the individual enzymes.
PROTEOLYTIC ENZYMES
A proteolytic enzyme is also sometimes known as protease, which, as explained earlier, is not a specific enzyme, but a type of enzyme. Proteases or proteolytic enzymes are simply enzymes that break down or digest protein. As explained earlier, there are proteolytic enzymes (proteases) that are also pancreatic enzymes, and there are proteolytic enzymes derived from plant sources.
The most potent pancreatic enzyme by far is called a-Chymotrypsin (also just called Chymotrypsin), which is also an anti-fibrolytic enzyme (an enzyme that is effective against dense fibrous tissue). Coming in second to Chymotrypsin as far as activity for a pancreatic enzyme is Trypsin. Although these are powerful protein-digesting enzymes, there are vegetable-based enzymes that break down protein as well. One of them, in particular, is a very potent anti-fibrolytic protease called Nattokinase, which is derived from the soy plant. The enzyme Bromelain is a proteolytic enzyme derived from pineapples, while Papain is a proteolytic enzyme derived from papaya. Both Bromelain and Papain are decent proteolytic enzymes. They are, in fact, much more resilient in the stomach than pancreatic enzymes, but they have a significantly reduced life span when compared to pancreatic enzymes. Pepsin and Bromelain are commonly found in digestive formulas, but they are also found in some systemic enzyme formulas as well. The most active proteolytic enzymes are most widely used in systemic enzyme formulas and MUST be enteric-coated to be effective. If they aren’t enteric-coated, they are subject to destruction from stomach acid. Even the vegetable-based proteolytic enzymes that survive the introduction of stomach acid must be enteric-coated and delivered directly to the duodenum if they are used in a formula designed for the absorption of the enzyme into the circulatory system.
It should be noted here that some are allergic to soy. However, there are rarely issues with allergic reactions to the soy-based enzyme, Nattokinase, by those who are allergic to soy. The reason for this is that most allergic reactions to soy are due to the proteins in soy. Nattokinase is a potent protein-digesting enzyme more than capable of breaking down any remaining protein residue in the extracted Nattokinase.
SERROPEPTASE & NATTOKINASE
There is another source of a very potent proteolytic enzyme that is neither a pancreatic source nor vegetable source, which is called Serratiopeptidase – more commonly known as Serropeptase. It is also known by several variations, such as Serratiapeptidase, Serrapeptidase, and some less common variations. For the sake of this discussion, we will refer to it as Serropeptase.
Serropeptase
Serropeptase was initially discovered and extracted from the silkworm, which was and still is a costly source. Now, it is by far more commonly extracted from ultra-purified fermenting bacteria. This source appears to be just as active as the silkworm extract, but with one potential concern. Research indicates serropeptase can help patients with chronic airway disease, lessening viscosity of sputum, and reducing coughing. Like lumbrokinase and nattokinase, serrapeptase breaks down fibrin. It also helps dissolve dead or damaged tissue without harming healthy tissue. There is a small percentage of people who are allergic to the bacteria in which Serropeptase is extracted. Although the fermented bacteria are heavily filtered, resulting in highly purified Serropeptase, some minuscule residue of the base remains with the enzyme. For the small percentage of people that are allergic to it, they cannot take Serropeptase without having an allergic reaction. The most common side effect is swelling of the face and neck. The allergic reaction usually disappears quickly once they stop taking fermented sourced Serropeptase. Serropeptase is argued by some to be one of the most potent anti-fibrolytic enzymes available, and most would agree on that.
Nattokinase
Produced by the bacteria Bacillus subtilis during the fermentation of soybeans to produce natto, nattokinase is a powerful thrombolytic and similar to aspirin, without the severe side effects.
Nattokinase is shown to break down blood clots and reduce the risk of serious clotting through dissolving excess fibrin in blood vessels, improving circulation, and decreasing the viscosity of the blood. In one particular in-vitro study, the thrombolytic activity of equivalent amounts of nattokinase and tPA was found to be identical.
Whether Nattokinase or Serropeptase is more potent, it seems to be clear that they are very close in enzyme activity. For these stated reasons, some prefer to produce supplements only with Nattokinase to avoid the issue with the small percentage that is allergic to fermented sourced Serropeptase.
Others manufacture a product that combines Nattokinase and Serropeptase, making the argument that they both have a purpose and that their functions are not identical. Most formulas that combine Nattokinase and pancreatic enzymes do not use Serropeptase for the previously stated reasons.
SYSTEMIC ENZYMES
Systemic enzymes are not a specific enzyme category. A systemic enzyme is a term that describes an enzyme or enzyme formula that is designed to be absorbed into the bloodstream and delivered to the entire body, or systemically if you will. Systemic enzymes are usually formulas that contain a mixture of pancreatic enzymes and vegetable source enzymes. What makes them systemic enzymes is the way that the formulas are explicitly designed to be delivered to and absorbed systemically in the duodenum as opposed to a digestive aid. There are a few ways that enzymes can be produced and/or utilized to be absorbed systemically. Still, only one method ensures that the integrity of the enzymes survives the destructive properties of stomach acid. In general, stomach acid is a good thing and is essential to proper digestion. However, it can destroy enzymes, particularly pancreatic enzymes, Natto-Kinase, Serropeptase, and others. Although fruit-based enzymes such as Bromelain and Papain will do just fine in stomach acid, they must also be enteric coated for maximum efficiency — if they are designed as a systemic enzyme.
One common technique used to get nutritive enzymes into the duodenum with as little damage as possible to the enzyme is to instruct the person taking them to be sure to take the enzymes on an empty stomach. Taking them on an empty stomach not only helps the enzyme to survive the stomach, but it also helps to get them into the system by not having them tied up digesting food. Even enteric-coated systemic enzyme formulas are best taken on an empty stomach. Usually, an empty stomach is defined as nothing to eat at least one hour before you take an enzyme tablet and/or do not take them for at least two hours after one has eaten. This works excellent for enteric-coated tablets, but only moderately well at best for non-enteric coated enzyme tablets, and is even less effective for non-enteric coated capsules than it is for tablets. When something is taken on an empty stomach, it will indeed stay in the stomach for a far shorter period on an empty stomach compared to a stomach that contains food. In theory, this protects the enzyme capsule from the stomach acid because it is being moved from the stomach to the duodenum much more rapidly. It definitely is being moved more quickly through the stomach, but how fast is it being moved is the question. There is little doubt that this technique does indeed greatly improve the amount of surviving enzymes through the stomach and into the alkaline-rich duodenum where it is absorbed.
The concern is that there is still a level of destruction that takes place in the stomach before the capsule arrives in the duodenum. Not a concern for most fruit-based enzymes, but it can be a severe concern for pancreatic based enzymes as well as others like Nattokinase and Serropeptase. It is an even bigger concern with non-enteric coated capsules for obvious reasons. A non-enteric coated capsule is very thin, and the contents are loosely packed. What is perceived as an advantage of capsules for herbs and other nutrients becomes a severe disadvantage to enzymes. Once the thin outer shell of a capsule is breached by stomach acid, the contents are also subjected to stomach acid and will easily be digested and destroyed. Again, when taken on an empty stomach, some, if not most of the contents of the capsule, will most likely reach the duodenum, and there will be some assimilation into the system. The concern is that the contents of the non-enteric coated capsule could be seriously depleted by the time it gets out of the acid-rich environment of the stomach and travels to the alkaline-rich environment of the duodenum.
Let’s Talk About Enteric-Coating
There is only one way to completely protect pancreatic (and other) enzymes through the stomach and ensure that they will be absorbed systemically. Only the utilization of an alkaline (ph) sensitive enteric coating will do the job. Unfortunately, many companies use a simple protein-based enteric coating that only works moderately well. The concern with using a simple protein coating is twofold. The first concern is that proteins are subject to digestion by stomach acid. Once the acid gets through the protein coating, it can begin to break down and destroy the enzymes it is “protecting”. The protein coating will definitely help the tablet get through the stomach better than a tablet/capsule that isn’t coated at all, especially if it is taken on an empty stomach. However, this brings up concern number two.
Sometimes the protein-based enteric coating helps the tablet/capsule survive the stomach. Still, unfortunately, it sometimes also “protects” it from being broken down in the duodenum where it is supposed to be absorbed.
A ph (alkaline) sensitive enteric coating guarantees the survival of the tablet/capsule through the stomach AND guarantees that the coating rapidly comes off in the duodenum. Stomach acid is not capable of digesting an alkaline (ph) sensitive coating. And unlike a simple protein coating, the alkaline (ph) sensitive enteric coating is explicitly designed to be broken down only when the tablet/capsule reaches a specific ph level. Once the tablet/capsule with the scientifically engineered coating reaches the specific alkalinity of the duodenum, the coating comes off very rapidly. Most coatings designed for duodenal absorption will come off in an alkaline environment where the ph is 6.7 or higher.
In contrast, the ph level of the stomach is typically about 1. This technology was pioneered by the German-based Mucos Corporation more than fifty years ago. They were using this technique on their well-known pancreatic enzyme formulas Wobenzyme and Wobe-Mugos long before anyone else even gave the enteric coatings a second thought. For years Mucos Corporation was the world leader in nutritional systemic enzyme sales because their products worked so much better than anyone else’s anywhere in the world. The secret was and is in the ph sensitive enteric coating, although it isn’t much of a secret anymore. Mucos Corporation still has an outstanding reputation and is still a leader in the industry with its Wobenzyme Med and Wobenzyme-N formulas. However, they no longer have an exclusive on the enteric coating that they pioneered, and they no longer have the most potent enzyme formula in the world. Mucos Corporation is mostly coasting on their well-deserved reputation but is still well respected in the industry. Univase Forte is the most potent systemic enzyme formula in the world with a scientifically engineered alkaline sensitive enteric coating for maximum absorption.
Why Supplement With Enzymes?
In a perfect world, we all would eat raw (organic) unprocessed foods that are naturally high in active enzymes. Unfortunately, we don’t live in an ideal world, especially when it comes to what we choose to eat.
The body can experience a challenging time keeping up with a chemical, processed-food overload that is also enzyme poor (cooking and processing destroy enzymes). We also neglect to chew our food adequately (saliva contains Amylase), so our body must find a way to compensate. The body must then redirect its production of metabolic proteolytic enzymes into the production of large amounts of pancreatic enzymes to help break down all of the dead food in our diet. In the short term, this is not a huge concern since the body is capable of handling it.
However, the long-term consequences of this redirection can be massive. It can lead to everything from a weakened immune system to thickened blood, from pain and inflammation to cardiovascular disease, and from decreased athletic performance to difficulty breathing. The easiest approach for many everyday conditions is to supplement with a systemic and digestive enzyme blend that will help digestion as well as support cardiovascular, immune, and metabolic health. When the body’s fundamental systems work well, aging slows down, and balance is easier to keep in check.
REFERENCES AND STUDIES
Greenberg RE, Holt PR. Influence of aging upon pancreatic digestive enzymes. Dig Dis Sci. 1986 Sep;31(9):970-7.
Miyasaka K, Kitani K. Aging impairs pancreatic response to refeeding following a protein-free diet. Pancreas. 1989;4(3): 346-52.
Wolfson D, Olmstead S, Meiss D, Ralston J. Making Sense of Digestive Enzymes: ProThera, Inc.;2008.
Glade MJ, Kendra D, Kaminski MV, Jr. Improvement in protein utilization in nursing-home patients on tube feeding supplemented with an enzyme product derived from Aspergillus niger and bromelain. Nutrition. 2001 Apr;17(4):348-50.
Karani S, Kataria MS, Barber AE. A double-blind clinical trial with a digestive enzyme product. Br J Clin Pract. 1971 Aug;25(8):375-7.
Wooldridge JL, Heubi JE, Amaro-Galvez R, ET AL. EUR-1008 pancreatic enzyme replacement is safe and effective in patients with cystic fibrosis and pancreatic insufficiency. J Cyst Fibros. 2009 Dec;8(6):405-17. Epub 2009 Aug 15.
Hammer HF. Pancreatic exocrine insufficiency: diagnostic evaluation and replacement therapy with pancreatic enzymes. Dig Dis. 2010;28(2):339-43. Epub 2010 Sep 1.
http://chemistry-today.teknoscienze.com/pdf/MU%20OMEGA3- 08.pdf Accessed October 1, 2012.
Stattin P, Bjor O, Ferrari P, Lukanova A, et al. Prospective study of hyperglycemia and cancer risk. Diabetes Care. 2007 Mar;30(3):561-7.
Vigneri P, Frasca F, Sciacca L, Pandini G, Vigneri R. Diabetes and cancer. Encocr Relat Cancer. 2009 Dec;16(4):1103-23.
Bash, LD, Selvin E, Steffes M, Coresh J, Astor BC. Poor glycemic control in diabetes and the risk of incident kidney disease even in the absence of albuminuria and retinopathy: atherosclerosis risk in communities (ARIC) study. Arch Intern Med. 2008 Dec 8;168(22):2440-7.
Held C, Gerstein HC, Zhao F, et al. Fasting plasma glucose is an independent predictor of hospitalization for congestive heart failure in high-risk patients. American Heart Association 2006 Scientific Sessions. November 13, 2006. Abstract 2562.
Healy L, Howard J, Ryan A, et al. Metabolic syndrome and leptin are associated with adverse pathological features in male colorectal cancer patients. Colorectal Dis. 2011 Jan 20.
Park HJ, Jung UJ, Cho SJ, Jung HK, Shim S, Choi MS. Citrus unshiu peel extract ameliorates hyperglycemia and hepatic steatosis by altering inflammation and hepatic glucose- and lipid-regulating enzymes in db/db mice. J Nutr Biochem. 2012 Jun 11. [Epub ahead of print]
Malik VS, Hu FB. Sweeteners and risk of obesity and Type 2 diabetes: The role of sugar-sweetened beverages. Curr Diab Rep. 2012 Jan 31. [Epub ahead of print]
Coutinho M, Gerstein H, Poque J, Wang Y, Yusuf S. The relationship between glucose and incident cardiovascular events: a metaregression analysis of published data from 20 studies of 95,783 individuals followed for 12.4 years. Diabetes Care. 1999 Feb;22(2):233-40.
Domínguez-Muñoz JE. Pancreatic exocrine insufficiency: diagnosis and treatment. J Gastroenterol Hepatol. 2011 Mar;26 Suppl 2:12-6.
Udani J, Hardy M, Madsen DC. Blocking carbohydrate absorption and weight loss: a clinical trial using Phase 2 brand proprietary fractionated white bean extract. Altern Med Rev. 2004 Mar;9(1):63-9.
Bergert FW, Conrad D, Ehrenthal K, et al. Pharmacotherapy guidelines for the aged by family doctors for the use of family doctors: Part D Basic conditions supporting drug treatment. Int J Clin Pharmacol Ther. 2009 May;47(5):289-302.
Evans WJ. Exercise and nutritional needs of elderly people: effects on muscle and bone. Gerodontology. 1998;15(1):15-24.
Ritz P. Factors affecting energy and macronutrient requirements in elderly people. Public Health Nutr. 2001 Apr;4(2B):561-8.
Remond D, Machebeuf M, Yven C, et al. Postprandial whole-body protein metabolism after a meat meal is influenced by chewing efficiency in elderly subjects. Am J Clin Nutr. 2007 May;85(5):1286-92.
Evans KE, Leeds JS, Morley S, Sanders DS. Pancreatic insufficiency in adult celiac disease: do patients require long-term enzyme supplementation? Dig Dis Sci. 2010 Oct;55(10):2999-3004.
Dominguez-Munoz JE. Pancreatic enzyme replacement therapy for pancreatic exocrine insufficiency: when is it indicated, what is the goal and how to do it? Adv Med Sci. 2011;56(1):1-5.
Roxas M. The role of enzyme supplementation in digestive disorders. Altern Med Rev. 2008 Dec;13(4):307-14.
Eun JS, Beauchemin KA. Effects of a proteolytic feed enzyme on intake, digestion, ruminal fermentation, and milk production. J Dairy Sci. 2005 Jun;88(6):2140-53.
Fiocchi A, Restani P, Riva E, et al. Meat allergy: II–Effects of food processing and enzymatic digestion on the allergenicity of bovine and ovine meats. J Am Coll Nutr. 1995 Jun;14(3):245-50.
Fuhrmann G, Leroux JC. In vivo fluorescence imaging of exogenous enzyme activity in the gastrointestinal tract. Proc Natl Acad Sci USA. 2011 May 31;108(22):9032-7. Epub 2011 May 16.
Shattock P, Whiteley P. Biochemical aspects in autism spectrum disorders: updating the opioid-excess theory and presenting new opportunities for biomedical intervention. Expert Opin Ther Targets. 2002 Apr;6(2):175-83.
Dangin M, Boirie Y, Garcia-Rodenas C, et al. The digestion rate of protein is an independent regulating factor of postprandial protein retention. Am J Physiol Endocrinol Metab. 2001 Feb;280(2):E340-8.
Dangin M, Boirie Y, Guillet C, Beaufrere B. Influence of the protein digestion rate on protein turnover in young and elderly subjects. J Nutr. 2002 Oct;132(10):3228S-33S.
Koopman R, Crombach N, Gijsen AP, et al. Ingestion of a protein hydrolysate is accompanied by an accelerated in vivo digestion and absorption rate when compared with its intact protein. Am J Clin Nutr. 2009 Jul;90(1):106-15.
Oben J, Kothari SC, Anderson ML. An open label study to determine the effects of an oral proteolytic enzyme system on whey protein concentrate metabolism in healthy males. J Int Soc Sports Nutr. 2008;5:10.
Omogbenigun FO, Nyachoti CM, Slominski BA. Dietary supplementation with multienzyme preparations improves nutrient utilization and growth performance in weaned pigs. J Anim Sci. 2004 Apr;82(4):1053-61.
Saha S, Verma R. Inhibitory potential of traditional herbs on α-amylase activity. Pharm Biol. 2012 Mar;50(3):326-31. Epub 2011 Dec 2.
Narita Y, Inouye K. Kinetic analysis and mechanism on the inhibition of chlorogenic acid and its components against porcine pancreas alpha-amylase isozymes I and II. J Agric Food Chem. 2009 Oct 14;57(19):9218-25.
Zentler-Munro PL, Assoufi BA, Balasubramanian K, et al. Therapeutic potential and clinical efficacy of acid-resistant fungal lipase in the treatment of pancreatic steatorrhoea due to cystic fibrosis. Pancreas. 1992;7(3):311-9.
Medhekar R. The first quantitative evidence proving the efficacy of supplemental enzymes: National Enzyme Company;2004.
Lin AH, Lee BH, Nichols BL, et al. Starch source influences dietary glucose generation at the mucosal α-glucosidase level. J Biol Chem. 2012 Sep 17. [Epub ahead of print]
Stevens CE, Hume ID. Contributions of microbes in vertebrate gastrointestinal tract to production and conservation of nutrients. Physiol Rev. 1998 Apr;78(2):393-427.
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