Enzyme Revolution

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Regular price: $59.99

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FULL DIGESTIVE SUPPORT*

Complete Profile of Digestive Enzymes*
Facilitates Natural Digestive Processes*
Enhances the Absorption of Nutrients*
30 Servings per Container

Quantity

Description

If you diet to meet your health goals, you are very concerned with digestion whether you realize it or not. Even minor disruptions to the digestive process are detrimental to any fitness or wellness goal. Having the support of a digestive enzyme complex like Enzyme Revolution can be the difference between almost and all the way. Maximizing nutrient absorption and gut function can improve things you may never even have noticed before, such as breathing, vision, and muscle strength. Of course, assisting the gut with supplemental enzymes also decreases the potential for bloating and other GI stressors.

Amylase and cellulase work to break down carbohydrates and fiber.*
Protease, pepsin, papain, and bromelain improve protein digestion and amino acid uptake.*
Lipase and pancreatin hydrolyze fats and minimize GI distress.*
Gentian reduces stomach discomfort and enhances natural nutrient absorption.*

Whether eating too much, too little, or just all the wrong foods (we’re all guilty sometimes!), Enzyme Revolution has your back. Want to eat a little ice cream but you know it bothers your stomach? Use Enzyme Revolution to reduce discomfort. Practicing an intermittent fasting diet? Take Enzyme Revolution during your feeding window to meet the intense demands of 3 plates of food per sitting. Bulking and eating 7 full meals per day? You should include Enzyme Revolution in your routine to make sure all those calories can be utilized.

Supplement Facts

Ingredient Profile

Betaine HCl

Similar to betaine anhydrous, an ergogenic aid, betaine HCl has a different function. Betaine HCl helps with digestion by donating HCl

Helps to break down foods in the stomach which is shown to increase vitamin and mineral absorption.
Only influences stomach acidity in the short term, will not lead to acid reflux.

Amylase

The amylase family, which consists of alpha-, beta-, and glucoamylase is a major enzyme in the breakdown of starches to smaller units.

The primary carbohydrate-digesting enzyme.
Hydrolyzes starch to maltose and isomaltose.
May help prevent high blood glucose levels.

Protease

Proteases break down proteins into short amino acid chains, which can then be further broken down into individual amino acids by other enzymes.

Essential for amino acid absorption from proteins.
May aid in tissue repair after exercise.

Pepsin

A specific protease, pepsin is present in the gut and formed when pepsinogen comes into contact with the acidity of the stomach.

The enzyme responsible for initial protein breakdown.
Capable of digesting the largest of proteins ingested.

Pancreatin

Pancreatin is a combination of several enzymes produced by the pancreas with the capacity for digestion of all macronutrients.

Papain

Papain is an enzyme from papaya that breaks down proteins. It is, therefore, a common ingredient in meat tenderizers. Papain hydrolyzes the peptide bonds in smaller peptides.

Digests long polypeptides into dipeptides and single amino acids.

Lipase

Lipase digests lipids (fats). It is responsible for breaking down the fats we consume in our diets, and too little lipase leads to digestive distress and disorders.

Relieves discomfort from bloating and gas.

Bromelain

Bromelain is a protease found in pineapple that profoundly helps digestion.

Cellulase

Cellulose is an insoluble fiber found in the cell wall of plants. Cellulase breaks down cellulose, and it is not common or robust in mammals (including humans), which is why we cannot digest fiber except by bacterial fermentation in the large intestine.

Turns fiber into utilizable monosaccharides.
May improve the nutritive value of fermented foods, grains, fruits, and vegetables.
Digests harmful microbial biofilms.

Gentian

Gentiana lutea is an herb used in traditional Chinese medicine used to treat stomach ailments and digestive complications. It may have over a dozen other therapeutic effects.

Promotes natural digestive enzyme action.
Extracts from Gentiana lutea have been found to improve endurance and reduce muscular fatigue.

FAQS

Q: What is the best way to use Digestive Nzymes Revolution?
A: As a dietary supplement, use 1 serving (2 capsules) of Digestive Nzymes Revolution prior to meals to aid the digestive process.

Q: Who should use Digestive Nzymes Revolution?
A: Anyone who experiences stomach discomfort from food, digestive symptoms like bloating, flatulence, or indigestion after eating, and those eating larger amounts of food to support athletic goals may find Digestive Nzymes Revolution helpful for relieving GI distress. If you are taking blood thinners or are allergic to pineapple, you should NOT use Digestive Nzymes Revolution.

Q: How does Digestive Nzymes Revolution work?
A: Digestive Nzymes Revolution supplies 10 ingredients known to participate in many aspects of the natural digestive process. This includes enzymes capable of digesting fats, proteins, and carbohydrates (including fiber). Digestion is a complex process with many steps from the mouth through the intestines, and Digestive Nzymes Revolution contains enzymes that act all along the natural spectrum.

References

Betaine HCl

1. Yago, M. R., Frymoyer, A. R., Smelick, G. S., Frassetto, L. A., Budha, N. R., Dresser, M. J., … & Benet, L. Z. (2013). Gastric reacidification with betaine HCl in healthy volunteers with rabeprazole-induced hypochlorhydria. Molecular Pharmaceutics, 10(11), 4032-4037.

2. Yago, M. R., Frymoyer, A., Benet, L. Z., Smelick, G. S., Frassetto, L. A., Ding, X., … & Dresser, M. J. (2014). The use of betaine HCl to enhance dasatinib absorption in healthy volunteers with rabeprazole-induced hypochlorhydria. The AAPS journal, 16(6), 1358-1365.

3. Aditi, A., & Graham, D. Y. (2012). Vitamin C, gastritis, and gastric disease: a historical review and update. Digestive diseases and sciences, 57(10), 2504-2515.

4. Recker, R. R. (1985). Calcium absorption and achlorhydria. New England Journal of Medicine, 313(2), 70-73.

5. Park, C. H., Kim, E. H., Roh, Y. H., Kim, H. Y., & Lee, S. K. (2014). The association between the use of proton pump inhibitors and the risk of hypomagnesemia: a systematic review and meta-analysis. PloS one, 9(11), e112558.

Amylase

1. Yadav, R., BhaRtiYa, J. P., Verma, S. K., & Nandkeoliar, M. K. (2013). The evaluation of serum amylase in the patients of type 2 diabetes mellitus, with a possible correlation with the pancreatic functions. Journal of clinical and diagnostic research: JCDR, 7(7), 1291.

2. Butterworth, P. J., Warren, F. J., & Ellis, P. R. (2011). Human α‐amylase and starch digestion: An interesting marriage. Starch‐Stärke, 63(7), 395-405.

Protease

1. Craik, C. S., Page, M. J., & Madison, E. L. (2011). Proteases as therapeutics. Biochemical Journal, 435(1), 1-16.

2. Shah, D., & Mital, K. (2018). The Role of Trypsin: Chymotrypsin in Tissue Repair. Advances in therapy, 1-12.

Pepsin

1. Roxas, M. (2008). The role of enzyme supplementation in digestive disorders. Altern Med Rev, 13(4), 307-14.

Pancreatin

1. Whitehead, A. M. (1988). Study to compare the enzyme activity, acid resistance and dissolution characteristics of currently available pancreatic enzyme preparations. Pharmaceutisch Weekblad, 10(1), 12-16.

2. Löhr, J. M., Hummel, F. M., Pirilis, K. T., Steinkamp, G., Körner, A., & Henniges, F. (2009). Properties of different pancreatin preparations used in pancreatic exocrine insufficiency. European journal of gastroenterology & hepatology, 21(9), 1024-1031.

Papain

1. Sharma, M., Sharma, V., Panda, A. K., & Majumdar, D. K. (2011). Development of enteric submicron particle formulation of papain for oral delivery. International journal of nanomedicine, 6, 2097.

Lipase

1. Lankisch, P. G., Burchard-Reckert, S., & Lehnick, D. (1999). Underestimation of acute pancreatitis: patients with only a small increase in amylase/lipase levels can also have or develop severe acute pancreatitis. Gut, 44(4), 542-544.

2. Groenemeijer, B. E., Hallman, M. D., Reymer, P. W., Gagné, E., Kuivenhoven, J. A., Bruin, T., … & Hayden, M. R. (1997). Genetic variant showing a positive interaction with β-blocking agents with a beneficial influence on lipoprotein lipase activity, HDL cholesterol, and triglyceride levels in coronary artery disease patients: the Ser447-stop substitution in the lipoprotein lipase gene. Circulation, 95(12), 2628-2635.

3. Mead, J. R., Irvine, S. A., & Ramji, D. P. (2002). Lipoprotein lipase: structure, function, regulation, and role in disease. Journal of molecular medicine, 80(12), 753-769.

Bromelain

1. Singh, T., More, V., Fatima, U., Karpe, T., Aleem, M. A., & Prameela, J. (2016). Effect of proteolytic enzyme bromelain on pain and swelling after removal of third molars. Journal of International Society of Preventive & Community Dentistry, 6(Suppl 3), S197.

2. Brien, S., Lewith, G., Walker, A., Hicks, S. M., & Middleton, D. (2004). Bromelain as a treatment for osteoarthritis: a review of clinical studies. Evidence-based complementary and alternative medicine, 1(3), 251-257.

3. Leeds, J. S., Hopper, A. D., Sidhu, R., Simmonette, A., Azadbakht, N., Hoggard, N., … & Sanders, D. S. (2010). Some patients with irritable bowel syndrome may have exocrine pancreatic insufficiency. Clinical Gastroenterology and Hepatology, 8(5), 433-438.

4. Fitzhugh, D. J., Shan, S., Dewhirst, M. W., & Hale, L. P. (2008). Bromelain treatment decreases neutrophil migration to sites of inflammation. Clinical Immunology, 128(1), 66-74.

Cellulase

1. Loiselle, M., & Anderson, K. W. (2003). The use of cellulase in inhibiting biofilm formation from organisms commonly found on medical implants. Biofouling, 19(2), 77-85.

2. Kumar, S. (2015). Role of enzymes in fruit juice processing and its quality enhancement. health, 6(6), 114-124.

3. Kapasakalidis, P. G., Rastall, R. A., & Gordon, M. H. (2009). Effect of a cellulase treatment on the extraction of antioxidant phenols from black currant (Ribes nigrum L.) pomace. Journal of Agricultural and Food Chemistry, 57(10), 4342-4351.

4. Tamang, J. P., Shin, D. H., Jung, S. J., & Chae, S. W. (2016). Functional properties of microorganisms in fermented foods. Frontiers in microbiology, 7, 578.

5. Singh, A., Karmakar, S., Jacob, B. S., Bhattacharya, P., Kumar, S. J., & Banerjee, R. (2015). Enzymatic polishing of cereal grains for improved nutrient retainment. Journal of food science and technology, 52(6), 3147-3157.

Gentian

1. Kesavan, R., Chandel, S., Upadhyay, S., Bendre, R., Ganugula, R., Potunuru, U. R., … & Joksic, G. (2016). Gentiana lutea exerts anti-atherosclerotic effects by preventing endothelial inflammation and smooth muscle cell migration. Nutrition, Metabolism and Cardiovascular Diseases, 26(4), 293-301.

2. Kesavan, R., Potunuru, U. R., Nastasijević, B., Avaneesh, T., Joksić, G., & Dixit, M. (2013). Inhibition of vascular smooth muscle cell proliferation by Gentiana lutea root extracts. PLoS One, 8(4), e61393.

3. Öztürk, N., Can Başer, K. H., Aydin, S., Öztürk, Y., & Çaliş, I. (2002). Effects of Gentiana lutea ssp. symphyandra on the central nervous system in mice. Phytotherapy Research: An International Journal Devoted to Pharmacological and Toxicological Evaluation of Natural Product Derivatives, 16(7), 627-631.

4. McMullen, M. K., Whitehouse, J. M., & Towell, A. (2015). Bitters: time for a new paradigm. Evidence-Based Complementary and Alternative

WARNING

California’s Proposition 65 entitles California consumers to special warnings.

WARNING: Cancer and Reproductive Harm - www.P65warnings.ca.gov/

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