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Best Digestive Enzyme Supplement

Digestive Enzymes™

Digestive Enzymes™



Optimal Digestive Support


  • Support Natural Digestive Processes*
  • Reduce Gastrointestinal Distress*
  • Completely Metabolize Foods*
  • Boost Nutrient Absorption*
  • 30 Servings






Our digestive system operates by using enzymes to breakdown foods into their utilizable components – amino acids, glucose, minerals, etc. Without sufficient enzymes, food continues to travel through the gastrointestinal tract to parts not equipped to digest foods. If food reaches the latter part of the digestive system, it creates bloating, flatulence, constipation, nausea and other disorders. Having sufficient enzymes, however, prevents issues due to indigestion.


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


Use Digestive Enzymes™ to help overcome specific food disagreements, obtain more nutrients from foods, and ease the digestive process.


*These statements have not been evaluated by the Food and Drug Administration. This product is not intended to diagnose, treat, cure, or prevent any disease.

Supplement Facts

 Best Digestive Enzyme Pill

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 correct hypochlorhydria (low stomach acid) to break down foods in the stomach.
  • Hypochlorhydria is linked to poor vitamin and mineral absorption.
  • Only influences stomach acidity in the short term, will not lead to acid reflux.



The amylase family, which consists of alpha-, beta-, and gluco-amylase 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.



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.
  • Proteases are currently being investigated as therapeutic agents for digestive disorders, inflammation, cystic fibrosis, and other diseases.
  • May aid in tissue repair after exercise.



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


  • Used to treat pancreatic problems that may arise from digestive system disorders
  • May help with food allergies.



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 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.
  • Lipase deficiencies are associated with acute pancreatitis.
  • Proper Lipase levels may prevent cardiovascular disorders.



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


  • May ameliorate symptoms of inflammatory bowel disease and ulcerative colitis.
  • Bromelain reduced swelling and pain following surgery, which may favorably translate to injuries as well.
  • Research on bromelain has found that it may be efficacious for attenuating symptoms of osteoarthritis.



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 nutritive value of fermented foods, grains, fruits, and vegetables.
  • Digests harmful microbial biofilms.



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.
  • May reduce endothelial inflammation, preventing atherosclerosis.
  • Extracts from Gentiana lutea have been found to improve endurance and reduce muscular fatigue.

Q: What is the best way to take Digestive Enzymes™?

A: As a dietary supplement, use 1 serving (2 capsules) of Digestive Enzymes™ prior to meals to aid the digestive process.


Q: Who should use Digestive Enzymes™?

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 Enzymes helpful for relieving GI distress. If you are taking blood thinners or are allergic to pineapple, you should NOT use Digestive Enzymes.


Q: How does Digestive Enzymes™ work?

A: Digestive Enzymes™ 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 Enzymes™ contains enzymes that act all along the natural spectrum.


Q: Can I stack Digestive Enzymes™ with other Optitune™ products for even greater digestive system function?

A: Yes, Digestive Enzymes™ pairs well with our Absorb and TUDCA products. Enzymes help break down foods into absorbable nutrients, and Absorb improves intestinal transporter function to pull nutrients from the digestive tract into the rest of the body. TUDCA supports the liver (the principal site of nutrient metabolism) in addition to the GI support from the enzymes.


Betaine HCl

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  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 journal16(6), 1358-1365.
  3. Aditi, A., & Graham, D. Y. (2012). Vitamin C, gastritis, and gastric disease: a historical review and update. Digestive diseases and sciences57(10), 2504-2515.
  4. Recker, R. R. (1985). Calcium absorption and achlorhydria. New England Journal of Medicine313(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 one9(11), e112558.


  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: JCDR7(7), 1291.
  2. Butterworth, P. J., Warren, F. J., & Ellis, P. R. (2011). Human α‐amylase and starch digestion: An interesting marriage. StarchStärke63(7), 395-405.


  1. Craik, C. S., Page, M. J., & Madison, E. L. (2011). Proteases as therapeutics. Biochemical Journal435(1), 1-16.
  2. Shah, D., & Mital, K. (2018). The Role of Trypsin: Chymotrypsin in Tissue Repair. Advances in therapy, 1-12.


  1. Roxas, M. (2008). The role of enzyme supplementation in digestive disorders. Altern Med Rev13(4), 307-14.


  1. Whitehead, A. M. (1988). Study to compare the enzyme activity, acid resistance and dissolution characteristics of currently available pancreatic enzyme preparations. Pharmaceutisch Weekblad10(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 & hepatology21(9), 1024-1031.


  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 nanomedicine6, 2097.


  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. Gut44(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. Circulation95(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 medicine80(12), 753-769.


  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 Dentistry6(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 medicine1(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 Hepatology8(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 immunology128(1), 66-74.


  1. Loiselle, M., & Anderson, K. W. (2003). The use of cellulase in inhibiting biofilm formation from organisms commonly found on medical implants. Biofouling19(2), 77-85.
  2. Kumar, S. (2015). Role of enzymes in fruit juice processing and its quality enhancement. health6(6), 114-124.
  3. Kapasakalidis, P. G., Rastall, R. A., & Gordon, M. H. (2009). Effect of a cellulase treatment on extraction of antioxidant phenols from black currant (Ribes nigrum L.) pomace. Journal of Agricultural and Food Chemistry57(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 microbiology7, 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 technology52(6), 3147-3157.


  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 Diseases26(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 One8(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 Derivatives16(7), 627-631.
  4. McMullen, M. K., Whitehouse, J. M., & Towell, A. (2015). Bitters: time for a new paradigm. Evidence-Based Complementary and Alternative Medicine2015.

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