You really shouldn’t…but that piece of cheesecake looks so good, and it’s been so long since you last had a slice — so you go for it. But shortly thereafter, you feel the rumbling of stomach and intestinal discontent, and — groan — you wish you had resisted.

A cast-iron stomach no more
When you were younger it seemed like you had a castiron stomach and could eat almost anything without having to pay the piper — but that’s not the case anymore, right? Now, indigestion, including heartburn, bloating and gas, seem to be the mainstay. And it’s especially true if you consume dairy products, grainbased foods (bread, pasta, etc.) containing gluten, or beans and greens (especially cruciferous vegetables like broccoli, cabbage and cauliflower). Look, it’s really not your fault. It’s due to your aging pancreas.

The old pancreas ain’t what it used to be The pancreas is the gland that secretes most of the enzymes you need to digest your food effectively. However, as you age, your pancreas begins to shrink.1 Not surprisingly, clinical research has shown that the effectiveness of the pancreas also reduces with age.2 The fact is, digestive enzyme secretion decreases in concentration as well as in output starting around age 303 — although it’s really after 40 that these changes become more noticeable. In one study, middle-aged subjects (40–70 years) had 30 percent less frequent secretion of digestive enzymes than subjects less than 40 years old, and elderly subjects (over 70) had 108 percent less frequent secretion of digestive enzymes than subjects less than 40 years old! Oh well, there’s nothing you can do about it. You just have to accept indigestion, right? Wrong. In fact, there’s a great deal you can do about it.

If your vision isn’t what it used to be, do you just accept it? Of course not — you get glasses or contacts and you see better again! Why wouldn’t you do the same thing with your enzymes? If you don’t make as much digestive enzymes as you used to, with indigestion being the result, don’t accept it as inevitable. You can compensate, with outstanding results!

Digestive enzymes
Supplementation with the right type of digestive enzymes can help you digest virtually any foods you eat, including those with dairy products and gluten. Ideally, you can use enzymes that act in two locations in your gastrointestinal tract: 1) your stomach, and 2) your small intestine. The result will likely be more optimum digestion with a happy stomach and gut.

Digestion in your stomach While most digestive enzymes work in the more alkaline environment of your intestines, pepsin is different. Pepsin is the digestive enzyme produced in the stomach and released there to work alongside hydrochloric acid to begin the process of digesting complex proteins in smaller protein chains. Without sufficient pepsin to perform this role, further digestion by pancreatic protein enzymes will be far less effective. However, as with pancreatic enzymes, pepsin secretion also decreases with age. In fact, people 65 and older were shown in research to have a 40 percent reduction in pepsin secretion. Consequently, supplementation with pepsin will help assure that this vital first step in protein digestion is optimized.

Digestion in your small intestine
The inadequate production of digestive enzymes from the pancreas can be addressed by supplementing with proteases (protein-digesting enzymes), amylases (starch-digesting enzymes) and lipases (fat-digesting enzymes). One popular source of such enzymes is pancreatin, an extract from the pancreas of cows or pigs. However, another effective sources are microbial enzymes, which have activities similar to pancreatin. Microbial enzymes have been the subject of various studies evaluating their effects on lactose intolerance, impaired pancreatic enzyme production, excess fat in the feces, celiac disorder and a variety of other digestive issues, with positive results.4,5,6,7,8,9

One of the most valuable attributes of microbial enzymes is that they appear to possess unusually high stability and activity throughout a wide range of pH conditions (from a pH of 2–10).10 This enables them to be more consistently active and functional for a longer distance as they are transported through the digestive tract. Also, since microbial enzymes are not derived from animal sources, they are perfectly appropriate for use by vegetarians — and research shows that are virtually non-toxic.11,12,13 Supplementation with a broad range of microbial proteases, amylases and lipases will safely and effectively assist in the digestion of protein, carbohydrates and fats from many food sources, including foods that contain dairy products, gluten, beans and greens.

Gluten sensitivity
Gluten (from Latin gluten, “glue”) is a mixture of proteins found in wheat, barley and rye.14 For many, gluten can be difficult to digest; with the result being gastrointestinal upset (abdominal pain and tenderness, irregular bowel habits: constipation or diarrhea or alternating bowel movements) as well as nongastrointestinal issues.15 The good news is that there is a combination of gluten digesting enzymes called Glutalytic, which has been tested in a double-blind, placebo-controlled study16 (the “gold standard” in research). The results showed a statistically significant improvement when compared to the placebo group in the following categories: pain, bloating, emptying of bowels, hunger pains, rumbling of stomach, lower energy levels, headaches, and food cravings.

Dairy sensitivity
Dairy sensitivity can be due to lactose intolerance, the inability to digest the milk sugar lactose, and/or difficulty in digesting milk proteins. The result may include gas, cramps, diarrhea or constipation.

Lactose intolerance is the result of the body discontinuing the production of the digestive enzyme lactase, which digests lactose. Since only one-third of all people retain the ability to digest lactose into adulthood, lactose intolerance is prevalent.17 Research has shown that supplementing with the lactase enzyme can reduce pain, bloating and total symptoms associated with lactose intolerance.18,19,20

The digestion of some milk proteins can take time. In fact, some research shows that a milk protein may remain in the stomach up to six hours before it is released into the intestines for further digestion.21 Difficulty in digesting milk proteins can result in constipation for some individuals.22 Luckily, supplementation with protease enzymes can help effectively digest milk proteins, thereby avoiding the effects of inadequate milk protein digestion.

Alpha-galactosidase
Bloating and gas are not fun to experience. Nevertheless, this experience is not unusual after eating beans and cruciferous vegetables (e.g. broccoli, cabbage and cauliflower). The reason is that these healthy foods contain goodly amounts of fiber, which can ferment in our gut. However, if these fibers can be broken down effectively, you’re less likely to experience bloating and gas. That’s where the enzyme alpha-galactosidase comes into play. In a double-blind, placebo-controlled study23 on intestinal gas production and gas-related symptoms, the microbial enzyme alpha-galactosidase was given to healthy volunteers after a meal containing about 15 ounces of cooked beans. The result was that there was a reduction in gas formation, severity of bloating, abdominal pain, discomfort, flatulence, and diarrhea. Beneficial results were also seen in a similar study.24

Conclusion
Indigestion, including heartburn, bloating and gas, are not fun. Avoiding foods that contain dairy and gluten, or even beans and cabbage, is likewise not fun. It may be possible to make your digestion more like it was when you were younger, with the use of a broad range of digestive enzymes.

Endnotes:
  1. Chantarojanasiri T, Hirooka Y, Ratanachu-Ek T, Kawashima H, Ohno E, Goto H. Evolution of pancreas in aging: degenerative variation or early changes of disease? J Med Ultrason (2001). 2015 Apr;42(2):177–83.
  2. Herzig K-H, Purhonen A-K, Räsänen KM, Idziak J, Juvonen P, Phillps R, Walkowiak J. Fecal pancreatic elastase-1 levels in older individuals without known gastrointestinal diseases or diabetes mellitus. BMC Geriatrics. 2011;11:4.
  3. Laugier R, Bernard JP, Berthezene P, Dupuy P. Changes in pancreatic exocrine secretion with age: pancreatic exocrine secretion does decrease in the elderly. Digestion. 1991;50(3-4):202–11.
  4. Alternative Medicine, the Definitive Guide. Future Medicine Publishing: Puyallup, WA. 1993;215–22.
  5. Griffin SM, et al. Acid resistant lipase as replacement therapy in chronic pancreatic exocrine insufficiency: a study in dogs. Gut 1989;30:1012–15.
  6. Schneider MU, et al. Pancreatic enzyme replacement therapy: comparative effects of conventional and enteric-coated microspheric pancreatin and acid-stable fungal enzyme preparations on steatorrhea in chronic pancreatitis. Hepato-gastroenterol 1985;32:97–102.
  7. Rosado JL, et al. Enzyme replacement therapy for primary adult lactase deficiency. Gastoenterol 1984;87:1072–82.
  8. Barillas C, Solomons NW. Effective reduction of lactose maldigestion in preschool by direct addition of beta-galactosidases to milk at mealtime. Pediatrics 1987;79(5):766–72.
  9. Phelan JJ, et al. Celiac disease: the abolition of gliadin toxicity by enzymes from Aspergillus niger. Clin Sci & Mol Med 1977;53:35–43.
  10. Griffin SM, et al. Acid resistant lipase as replacement therapy in chronic pancreatic exocrine insufficiency: a study in dogs. Gut 1989;30:1012–15.
  11. Garvin, P.J. & Merubia, J. Unpublished report. Submitted to WHO by Baxter Laboratories, Inc; 1959.
  12. Garvin, P.J., Willard, R., Merubia, J., Huszar, B., Chin, E., & Gilbert, C. Unpublished report. Submitted to WHO by Baxter Laboratories, Inc; 1966.
  13. Garvin, P.J., Ganote, C.E., Merubia, J., Delahany, E., Bowers, S., Varnado, A., Jordan, L., Harley, G., DeSmet, C., & Porth, J. Unpublished report from Travenol Laboratories, Inc., Morton Grove, IL, USA. Submitted to WHO by Gist-brocades NV, Delft, Holland; 1972.
  14. Lamacchia C, Camarca A, Picascia S, Di Luccia A, Gianfrani C. Cereal-based gluten-free food: how to reconcile nutritional and technological properties of wheat proteins with safety for celiac disease patients. Nutrients. 2014 Jan 29;6(2):575–90.
  15. Mansueto P, Seidita A, D’Alcamo A, Carroccio A. Non-celiac gluten sensitivity: literature review. J Am Coll Nutr. 2014;33(1):39–54.
  16. Hudson M, King C. Glutalytic Clinical Trial for Normal Consumption of Gluten Containing Foods. Department of Biology, Kennesaw State University, Kennesaw Georgia. 2015: 4 pgs.
  17. Gudmand-Hoyer E. The clinical significance of disaccharide maldigestion. Am J Clin Nutr 1994; 59(3):735S–41S.
  18. Ramirez FC, Lee K, Graham DY. All lactase preparations are not the same: results of a prospective, randomized, placebo-controlled trial. Am J Gastroenterol 1994;89:566–70.
  19. Sanders SW, Tolman KG, Reitberg DP. Effect of a single dose of lactase on symptoms and expired hydrogen after lactose challenge in lactoseintolerant subjects. Clin Pharm 1992;11:533–8.
  20. Lin MY, Dipalma JA, Martini MC, et al. Comparative effects of exogenous lactase (beta-galactosidase) preparations on in vivo lactose digestion. Dig Dis Sci 1993;38:2022–7.
  21. Ross RP, Fitzgerald GF, Stanton C. Unraveling the digestion of milk protein. Am J Clin Nutr. 2013 Jun;97(6):1161–2.
  22. Daher S, Tahan S, Solé D, Naspitz CK, Da Silva Patrício FR, Neto UF, De Morais MB. Cow’s milk protein intolerance and chronic constipation in children. Pediatr Allergy Immunol. 2001 Dec;12(6):339–42.
  23. Di Stefano M, Miceli E, Gotti S, Missanelli A, Mazzocchi S, Corazza GR.The effect of oral alpha-galactosidase on intestinal gas production and gas-related symptoms. Dig Dis Sci 2007;52(1):78–83.
  24. Patil AG, Kote NV, Mulimani V. Enzymatic removal of flatulence-inducing sugars in chickpea milk using free and polyvinyl alcohol immobilized alpha-galactosidase from Aspergillus oryzae. J Ind Microbiol Biotechnol
2009;36(1):29–33.