Digestive Enzyme Guide

For your convenience, we have compiled a list of the 20 most popular digestive enzymes.

This list of digestive enzymes and their benefits does not contain all known digestive enzymes, only ones that you are the most likely to encounter.

The following guide contains enzymes which have been researched and are classified as safe and effective.



 May be used to treat complex carbohydrate intolerance; Alleviates  gassiness(1)



 Breaks complex carbohydrates down into smaller chains, or even into  simple  sugars to be used as energy(2)



 Helps digest cellulose plant fiber, cereal bran fiber, and parts of certain  types  of fungi, yeast, and bacteria(3)



 Treats indigestion; Reduces inflammation(4)



 Helps digest plant matter(5)



 Diastase transforms starch into maltose, then converts it into usable  energy(6)



 Helps with the absorption of Vitamin B12(7)



 Helps digest plant matter(8)



 Helps digest Sucralose (table sugar)(9)



 Converts lactose into usable energy. This enzyme decreases with age. As  such  lactose intolerance is common among the older population,  manifesting with  bloating, abdominal pain, and diarrhea.(10)



 Helps digest lipids and fat(11)



 Prevents the growth of disease-causing organisms in newborns; Offsets the  infection susceptibility of diabetic Hyperglycemia(12)




 Breaks down pectin, a polysaccharide found in plant cell walls one of the  most studied and widely used commercial pectinases(14)



 Pepsin breaks down the protein in the food into smaller particles, such as  peptide fragments and amino acids(15)



 Helps digest grains and oil seeds(16)



 Breaks down amino acids for absorption(17)


Protease DPP IV

 Has been shown to lessen or eliminate allergic reactions to gluten(18)*



 Breaks down Sucralose (table sugar) into usable energy(19)



 Helps digest plant matter(20)






  1. Ganiats, Theodore G., et al. “Does Beano prevent gas?: a double-blind crossover study of oral alpha-galactosidase to treat dietary oligosaccharide intolerance.” Journal of Family Practice Nov. 1994: 441+. Academic OneFile. Web. 9 Sept. 2016.
  2. “Anthera Pharmaceuticals – Sollpura.” Anthera Pharmaceuticals – Sollpura. N.p., n.d. Web. 21 July 2015.<http://www.anthera.com/pipeline/science/sollpura.html>.
  3. Adams DJ. Fungal cell wall chitinases and glucanases. Microbiology. 2004 Jul;150(Pt 7):2029-35. Review.
  4. “Bromelain”. National Center for Complementary and Integrative Health, US National Institutes of Health. 20 April 2016. Retrieved24 April 2016.
  5. Worthington Biochemical Corporation (2014), Cellulase. Accessed on 2014-07-03
  6. Gray, G.M. (1975). “Carbohydrate digestion and absorption”. New England Journal of Medicine. 292 (23): 1225–1230. doi:10.1056/NEJM197506052922308. PMID 1093023.
  7. Morkbak AL, Poulsen SS, Nexo E (2007). “Haptocorrin in humans”.Clinical Chemistry and Laboratory Medicine. 45 (12): 1751–9.doi:10.1515/CCLM.2007.343. PMID 17990953.
  8. “Hemicellulase”. GMO Compass. 14 Feb 2008. Web. 9 Sept. 2016.<http://www.gmo-compass.org/eng/database/enzymes/88.hemicellulase.html>.
  9. Myrbäck, K. (1960). “Invertases”. In Boyer, P.D.; Lardy, H.; Myrbäck, K. The Enzymes. 4 (2nd ed.). New York: Academic Press. pp. 379–396.
  10. Järvelä I, Torniainen S, Kolho KL (2009). “Molecular genetics of human lactase deficiencies”. Annals of Medicine. 41 (8): 568–75. doi:10.1080/07853890903121033.PMID 19639477.
  11. Svendsen A (2000). “Lipase protein engineering”. Biochim Biophys Acta. 1543 (2): 223–228. doi:10.1016/S0167-4838(00)00239-9.PMID 11150608.
  12. Yoshimura K, Toibana A, Nakahama K (January 1988). “Human lysozyme: sequencing of a cDNA, and expression and secretion by Saccharomyces cerevisiae”. Biochem. Biophys. Res. Commun. 150 (2): 794–801. doi:10.1016/0006-291X(88)90461-5.PMID 2829884.
  13. (Spot was Mucin)
  14. Enzyme India, Pectinase. Available in: http://www.enzymeindia.com/enzymes/pectinase.asp. Accessed on 09/10/2008.
  15. Dunn BM (Nov 2001). “Overview of pepsin-like aspartic peptidases”. Current Protocols in Protein Science. Chapter 21: Unit 21.3. doi:10.1002/0471140864.ps2103s25.ISBN 0471140864. PMID 18429164.
  16. Mullaney EJ, Daly CB, Ullah AH (2000). “Advances in phytase research”. Adv Appl Microbiol. 47: 157–199. doi:10.1016/S0065-2164(00)47004-8. PMID 12876797.
  17. Hooper, ed. by N. M. (2002). Proteases in biology and medicine. London: Portland Press. ISBN 1-85578-147-6.
  18. “DPP-IV Enzymes: Clearing Up the Confusion about Activity Units”. Klaire. 2010. Web 9 Sep. 2016. http://www.klaire.com/images/dppiv_update_article.pdf
  19. Hubert Schiweck, Margaret Clarke, Günter Pollach “Sugar” in Ullmann’s Encyclopedia of Industrial Chemistry 2007, Wiley-VCH, Weinheim. doi:10.1002/14356007.a25_345.pub2
  20. Beg, Q. K.; Kapoor, M.; Mahajan, L.; Hoondal, G. S. (2001). “Microbial xylanases and their industrial applications: A review”. Applied Microbiology and Biotechnology. 56 (3–4): 326–38. doi:10.1007/s002530100704.PMID 11548999.