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Flatulence is not funny for those who suffer
Shall we chat about flatulence? Given the time spent on this topic in comedy routines, you’d think it was hilarious. But it’s not that funny for people who suffer from the embarrassment and discomfort of excessive gas.
A multinational survey, including nearly 6,000 people, recently showed that flatulence affects 81% of the adult population.[1] Many participants also suffered from stomach rumbling, belching, bloating, and trapped wind. Remarkably, only 11% of the respondents had no gas symptoms.
The lead author, Professor Olafur Palsson from the University of North Carolina, said: “I think the most remarkable and surprising finding in our study is that almost all adults in the general population experience some daily gas-related symptoms. This is important given the data also clearly reveals that these symptoms affect people’s general well being. Having a high amount of these common intestinal symptoms is associated with higher levels of depression, anxiety and stress, as well as impaired general quality of life.”[1]
A variety of conditions are associated with excessive gas: small intestinal bacterial overgrowth (SIBO), celiac disease, and pancreatitis, among others. Tests are available for these and other conditions, so if you have gastrointestinal issues of any kind, it’s worth consulting a health professional in order to rule out any underlying medical conditions.[2],[3]
Flatulence varies from person to person depending on many factors, including diet, the microbiome, and inherent digestive capacity.[4],[5],[6] In many cases, excessive flatulence may be caused by incomplete digestion, in which case supplemental digestive enzymes may help.
Insufficient digestion as a cause of excessive gas
Insufficient digestion is a very common cause of intestinal gas and bloating.
Insufficient digestion is a very common cause of intestinal gas and bloating.[7],[8],[9],[10] If carbohydrates and proteins are not completely digested in the stomach and small intestine, they end up in the bowel, where they are fermented by bacteria.[6],[11]
Bacterial fermentation of carbohydrates produces small molecules (some of which are beneficial, like short-chain fatty acids) and odorless gases, such as carbon dioxide and methane, which are released as flatulence.[12] The fermentation of proteins, however, produces hydrogen sulfide (H2S), which smells like rotten eggs (more about this below).
Inadequate digestion causes gastrointestinal problems when certain foods are consumed, leading to food intolerance.
Foods that often produce flatulence include milk and dairy products; legumes (beans, soy, lentils, and peas); vegetables (such as cabbage, Brussels sprouts, broccoli, cauliflower, asparagus, onions, and turnips); fruits (especially apples, pears, peaches, apricots and plums); and whole grains (including wheat, rye and barley).[13],[14],[15],[16]
Food intolerances are often addressed by changing one’s diet to remove the offending foods. However, eliminating fiber-containing foods can change the microbiome in an unhealthy way.
Supplemental digestive enzymes can support the breakdown, absorption, and utilization of hard-to-digest carbohydrates, proteins, and plant fibers for individuals with mild digestive abnormalities, food intolerances or excessive gas, as discussed below.
Milk intolerance
Oral lactase supplementation can help relieve symptoms of lactose intolerance.
Milk and other dairy products contain lactose, a disaccharide that makes up around 2–8% of milk by weight.[17] Lactose is normally cleaved in the small intestine by an enzyme called lactase (also known as β-galactosidase).[9],[18] The two components of lactose, glucose and galactose, are then absorbed and used for energy in the rest of the body.
Lactase activity is plentiful in infants and children, but its activity drops in adulthood.[19] When lactose is not completely digested it becomes available for fermentation in the colon, resulting in excessive flatulence and other symptoms.[18],[19],[20],[21] In a recent study, 54% of individuals diagnosed with irritable bowel syndrome (IBS) were actually found to have lactose intolerance.[22]
Lactose intolerance is determined by assessing abdominal symptoms (pain, bloating, gas and/or diarrhea) after lactose ingestion.[11],[21],[23],[24] Oral lactase supplementation can help relieve symptoms of lactose intolerance.[18],[25],[26]
Milk intolerance also occurs due to proteins known as caseins.[27],[28],[29] An enzyme that is normally produced in the intestines, DPP-IV, is necessary for the digestion of caseins and may improve milk tolerance.[30],[31],[32]
Non-celiac gluten sensitivity
Improved digestion of gluten has been achieved by combining DPP-IV with a proline-specific enzyme known as aspergillopepsin.
Dietary gluten causes problems for people with celiac disease, wheat allergy, and non-celiac gluten sensitivity (NCGS).[33] People with celiac disease need to avoid gluten entirely, as even a small amount can damage intestinal tissues. A simple blood test is used to diagnose celiac disease.
NCGS occurs when there is incomplete digestion of wheat and related cereals. NCGS is associated with gas, bloating, abdominal pain, and other symptoms triggered by those foods.[34],[35] The carbohydrates in grains can also trigger symptoms, so “non-celiac wheat sensitivity” may be a more accurate term.[36],[37]
Improved digestion of gluten has been achieved by combining DPP-IV with a proline-specific enzyme from Aspergillus niger, known as aspergillopepsin.[38] In humans, supplementation with these enzymes resulted in the complete breakdown of approximately one gram of gluten before it reached the small intestine.[38] The enzymes improved NCGS symptoms in otherwise healthy adults in placebo-controlled trials.[39],[40],[41]
Mild pancreatic enzyme insufficiency
Mild pancreatic insufficiency can contribute to food intolerances and excessive gas production.
Pancreatic enzymes (amylase, proteases, and lipase) are essential for the normal breakdown of carbohydrates, proteins and fats, respectively.[42],[43],[44] Pancreatic enzymes are secreted into the small intestine in response to a meal.
If pancreatic enzymes are inadequate, partially digested proteins pass into the colon where they are fermented by bacteria, producing smelly H2S, ammonia, and other byproducts.[6],[45],[46],[47],[48] Excessive H2S levels contribute to irritable bowel syndrome.[49]
Pancreatic enzymes decline with age, beginning at about age 30.[50],[51],[52] Mild pancreatic insufficiency can contribute to food intolerances, excessive gas production, and symptoms resembling IBS.[53],[54],[55] Supplemental enzymes may aid in normal digestion of fats and proteins and relieve symptoms.[56],[57],[58]
Principles of digestive enzyme supplementation
It is important to take digestive enzymes at the beginning of the meal so that they are available during the first hour of digestion.
It is important to take digestive enzymes at the beginning of the meal so that they are available during the first hour of digestion.[26],[59],[60] Here are some of the supplemental enzymes that have been used:
- Amylase: This enzyme, present in saliva and in pancreatic fluid, breaks down carbohydrates (starch) into sugars which are more easily absorbed by the body.[61]
- Lactase (beta-galactosidase): Lactase is responsible for digesting the lactose present in milk. Supplemental lactase is often helpful for people with lactose intolerance.[26],[59]
- Alpha-galactosidase: This enzyme breaks down galactooligosaccharides (GOS) and raffinose family oligosaccharides found in legumes (beans) and GOS-containing vegetables.[62],[63],[64],[65] Alpha-galactosidase taken with foods has been shown to relieve symptoms in GOS-sensitive individuals.[66]
- Peptidase (DPP-IV): This enzyme plays a significant role in the digestion of proline-containing peptides, including those found in milk and wheat.[30],[38]
- Aspergillopepsin: This protease breaks down the proline-rich peptides from gluten, and may alleviate non-celiac gluten sensitivity (NCGS), especially if taken in combination with DPP-IV.[38],[67],[68]
- Lipase: This pancreatic enzyme works with bile from the liver to break down fat molecules so they can be absorbed and used by the body. Lipase can aid in the digestion of high-fat meals.[16],[58]
Last but not least, the microbiome is a key player in the development of flatulence,[69] and probiotic supplementation has been suggested to improve food intolerances.[70],[71],[72] A combination of digestive enzymes with probiotics may be helpful for people who suffer from excessive flatulence but are otherwise healthy.
If you enjoyed this article, you may also be interested in the following posts:
Are Gluten-Free Diets Just a Fad? Understanding celiac disease, wheat allergy, non-celiac gluten sensitivity, & other gluten-related disorders.
Can Probiotics Soothe IBS? Evidence supports the use of probiotics for IBS and enhanced quality of life.
Constipation: Solutions to Make All Systems “Go”! Supporting the nervous system, microbiome, and nutritional status for healthy, easy elimination.
[1] EurekAlert. Gas-related intestinal symptoms affect nearly all adults on a daily basis, and are associated with psychological distress and poorer quality of life, new multi-national survey finds [Internet]. Vienna: United European Gastroenterology; 2021 [cited 2022 Feb 10]. Available from: https://www.eurekalert.org/news-releases/929709
[2] Schiller LR. Maldigestion versus malabsorption in the elderly. Curr Gastroenterol Rep. 2020 Jun 4;22(7):33.
[3] Wilkinson JM, et al. Gas, bloating and belching: approach to evaluation and management. Am Fam Physician. 2019 Mar 1;99(5):301-9.
[4] Malagelada JR, et al. Bloating and abdominal distension: old misconceptions and current knowledge. Am J Gastroenterol. 2017 Aug;112(8):1221-31.
[5] Bolin TD, Stanton RA. Flatus emission patterns and fibre intake. Eur J Surg Suppl. 1998;(582):115-8.
[6] Dallas DC, et al. Personalizing protein nourishment. Crit Rev Food Sci Nutr. 2017 Oct 13;57(15):3313-31.
[7] Keller J, Layer P. The pathophysiology of malabsorption. Viszeralmedizin. 2014;30:150-4.
[8] Sullivan SN. Functional abdominal bloating with distention. ISRN Gastroenterol. 2012;2012:721820.
[9] Lomer MC. Review article: the aetiology, diagnosis, mechanisms and clinical evidence for food intolerance. Aliment Pharmacol Ther. 2015;41:262-75.
[10] Raithel M, et al. The malabsorption of commonly occurring mono and disaccharides: levels of investigation and differential diagnoses. Dtsch Arztebl Int. 2013;110:775-82.
[11] Grabitske HA, Slavin JL. Gastrointestinal effects of low-digestible carbohydrates. Crit Rev Food Sci Nutr. 2009;49:327-60.
[12] Hasler WL. Gas and bloating. Gastroenterol Hepatol (N Y). 2006 Sep;2(9):654-62.
[13] Muir JG, et al. Measurement of short-chain carbohydrates in common Australian vegetables and fruits by high-performance liquid chromatography (HPLC). J Agric Food Chem. 2009;57:554-65.
[14] Van den Ende W. Multifunctional fructans and raffinose family oligosaccharides. Front Plant Sci. 2013;4:247.
[15] Cuomo R, et al. Irritable bowel syndrome and food interaction. World J Gastroenterol. 2014;20:8837-45.
[16] Money ME, et al. Pilot study: a randomised, double blind, placebo-controlled trial of pancrealipase for the treatment of postprandial irritable bowel syndrome-diarrhoea. Frontline Gastroenterol. 2011;2:48-56.
[17] Lin AH, et al. Unexpected high digestion rate of cooked starch by the Ct-maltase-glucoamylase small intestine mucosal α-glucosidase subunit. PLoS One. 2012;7:e35473.
[18] Ibba I, et al. Effects of exogenous lactase administration on hydrogen breath excretion and intestinal symptoms in patients presenting lactose malabsorption and intolerance. BioMed Research International. 2014;2014:680196.
[19] Di Rienzo T, et al. Lactose intolerance: from diagnosis to correct management. Eur Rev Med Pharmacol Sci. 2013;17 Suppl 2:18-25.
[20] Deng Y, et al. Lactose intolerance in adults: biological mechanism and dietary management. Nutrients. 2015;7:8020-35.
[21] Wilder-Smith CH, et al. Fructose and lactose intolerance and malabsorption testing: the relationship with symptoms in functional gastrointestinal disorders. Aliment Pharmacol Ther. 2013;37:1074-83.
[22] Poon D, et al. A systematic review and meta-analysis on the prevalence of non-malignant, organic gastrointestinal disorders misdiagnosed as irritable bowel syndrome. Sci Rep. 2022 Feb 4;12(1):1-6.
[23] Misselwitz B, et al. Lactose malabsorption and intolerance: pathogenesis, diagnosis and treatment. United European Gastroenterol J. 2013;1:151-9.
[24] Schiffner R, et al. Do patients with lactose intolerance exhibit more frequent comorbidities than patients without lactose intolerance? An analysis of routine data from German medical practices. Ann Gastroenterol. 2016;29:174-9.
[25] Sanders SW, et al. Effect of a single dose of lactase on symptoms and expired hydrogen after lactose challenge in lactose-intolerant subjects. Clin Pharm. 1992 Jun;11(6):533-8.
[26] Gao KP, et al. Effect of lactase preparations in asymptomatic individuals with lactase deficiency-gastric digestion of lactose and breath hydrogen analysis. Nagoya J Med Sci. 2002 May 1;65(1/2):21-8.
[27] Jiangin S, et al. Effects of milk containing only A2 beta casein versus milk containing both A1 and A2 beta casein proteins on gastrointestinal physiology, symptoms of discomfort, and cognitive behavior of people with self-reported intolerance to traditional cows’ milk. Nutr J. 2016;15:35.
[28] Pal S, et al. Milk intolerance, beta-casein and lactose. Nutrients. 2015;7:7285-97.
[29] Woodford KB. Casomorphins and gliadorphins have diverse systemic effects spanning gut, brain and internal organs. Int J Environ Res Public Health. 2021 Jul 26;18(15):7911.
[30] Nongonierma AB, FitzGerald RJ. Susceptibility of milk protein-derived peptides to dipeptidyl peptidase IV (DPP-IV) hydrolysis. Food Chem. 2014;145:845-52.
[31] Tiruppathi C, et al. Genetic evidence for role of DPP IV in intestinal hydrolysis and assimilation of prolyl peptides. Am J Physiol. 1993 Jul;265(1 Pt 1):G81-9.
[32] Arisoy S, Üstün-Aytekin Ö. Hydrolysis of food-derived opioids by dipeptidyl peptidase IV from Lactococcus lactis spp. Lactis. Food Res Int. 2018 Sep;111:574-581.
[33] Beyond Celiac. Non-celiac gluten sensitivity [Internet]. Ambler (PA): Beyond Celiac; 2020 [cited 2022 Feb 10]. Available from: https://www.beyondceliac.org/celiac-disease/non-celiac-gluten-sensitivity/
[34] Aufiero VR, et al. Non-celiac gluten sensitivity: how its gut immune activation and potential dietary management differ from celiac disease. Mol Nutr Food Res. 2018 May;62(9):e1700854.
[35] Catassi C, et al. Non-celiac gluten sensitivity: the new frontier of gluten related disorders. Nutrients. 2013 Sep 26;5(10):3839-53.
[36] Gargano D, et al. Food allergy and intolerance: a narrative review on nutritional concerns. Nutrients. 2021 May 13;13(5):1638.
[37] Skodje GI, et al. Fructan, rather than gluten, induces symptoms in patients with self-reported non-celiac gluten sensitivity. Gastroenterology. 2018 Feb;154(3):529-39.
[38] Ehren J, et al. A food-grade enzyme preparation with modest gluten detoxification properties. PLoS One. 2009 Jul 21;4(7):e6313.
[39] Maher M, et al. A glutalytic enzyme supplement was tolerated by healthy young adults. Food Nutr Sci. 2018 Feb 23;9(02):99.
[40] Deaton J, et al. Tolerance and efficacy of Glutalytic™: a randomized, double-blind, placebo-controlled study. J Nutr Food Sci. 2018;8:5.
[41] Dunaevsky YE, et al. Effective degradation of gluten and its fragments by gluten-specific peptidases: a review on application for the treatment of patients with gluten sensitivity. Pharmaceutics. 2021 Oct 2;13(10):1603.
[42] Pezzilli R, et al. Exocrine pancreatic insufficiency in adults: a shared position statement of the Italian Association for the Study of the Pancreas. World J Gastroenterol. 2013;19:7930-46.
[43] Armand M. Lipases and lipolysis in the human digestive tract: where do we stand? Curr Opin Clin Nutr Metab Care. 2007;10:156-64.
[44] Fieker A, et al. Enzyme replacement therapy for pancreatic insufficiency: present and future. Clin Exp Gastroenterol. 2011;4:55-73.
[45] Webster AD, et al. Influence of short-term changes in dietary sulfur on the relative abundances of intestinal sulfate-reducing bacteria. Gut Microbes. 2019;10(4):447-57.
[46] Yao CK, et al. Review article: insights into colonic protein fermentation, its modulation and potential health implications. Aliment Pharmacol Ther. 2016;43:181-96.
[47] Blachier F, et al. Cysteine-derived hydrogen sulfide and gut health: a matter of endogenous or bacterial origin. Curr Opin Clin Nutr Metab Care. 2019 Jan;22(1):68-75.
[48] Geypens B, et al. Influence of dietary protein supplements on the formation of bacterial metabolites in the colon. Gut. 1997 Jul;41(1):70-6.
[49] Singh SB, Lin HC. Hydrogen sulfide in physiology and diseases of the digestive tract. Microorganisms. 2015 Nov 12;3(4):866-89.
[50] Laugier R, et al. Changes in pancreatic exocrine secretion with age: pancreatic exocrine secretion does decrease in the elderly. Digestion. 1991;50:202-11.
[51] Rothenbacher D, et al. Prevalence and determinants of exocrine pancreatic insufficiency among older adults: results of a population-based study. Scand J Gastroenterol. 2005;40:697-704.
[52] Herzig KH, et al. Fecal pancreatic elastase-1 levels in older individuals without known gastrointestinal diseases or diabetes mellitus. BMC Geriatr. 2011;11:4.
[53] Soenen S, et al. The ageing gastrointestinal tract. Curr Opin Clin Nutr Metab Care. 2016 Jan;19(1):12-8.
[54] Leeds JS, et al. Some patients with irritable bowel syndrome may have exocrine pancreatic insufficiency. Clin Gastroenterol Hepatol. 2010;8:433-8.
[55] Singh VK, et al. Less common etiologies of exocrine pancreatic insufficiency. World J Gastroenterol. 2017 Oct 21;23(39):7059-76.
[56] Campbell JA, et al. Should we investigate gastroenterology patients for pancreatic exocrine insufficiency? A dual centre UK study. J Gastrointestin Liver Dis. 2016 Sep;25(3):303-9.
[57] Campbell JA, et al. PWE-208 How common is pancreatic exocrine insufficiency in primary care? Gut. 2015;64(Suppl 1):A303.
[58] Levine ME, et al. Lipase supplementation before a high-fat meal reduces perceptions of fullness in healthy subjects. Gut Liver. 2015 Jul;9(4):464-9.
[59] Ianiro G, et al. Digestive enzyme supplementation in gastrointestinal diseases. Curr Drug Metab. 2016;17:187-93.
[60] Trang T, et al. Pancreatic enzyme replacement therapy for pancreatic exocrine insufficiency in the 21(st) century. World J Gastroenterol. 2014 Sep 7;20(33):11467-85.
[61] Butterworth PJ, et al. Human α‐amylase and starch digestion: an interesting marriage. Starch‐Stärke. 2011 Jul;63(7):395-405.
[62] Adya S, Elbein AD. Glycoprotein enzymes secreted by Aspergillus niger: purification and properties of alpha-glaactosidase. J Bacteriol. 1977;129:850-6.
[63] DiPierro F, et al. A pilot trial on subjects with lactose and/or oligosaccharides intolerance treated with a fixed mixture of pure and enteric-coated α- and β-galactosidase. Clin Exp Gastroenterol. 2015;8:95-100.
[64] DiNardo G, et al. Efficacy and tolerability of α-galactosidase in treating gas-related symptoms in children: a randomized, double-blind, placebo controlled trial. BMC Gastroenterol. 2013;13:142.
[65] Levine B, Weisman S. Enzyme replacement as an effective treatment for the common symptoms of complex carbohydrate intolerance. Nutr Clin Care. 2004;7:75-81.
[66] Tuck CJ, et al. Increasing symptoms in irritable bowel symptoms with ingestion of galacto-oligosaccharides are mitigated by α-galactosidase treatment. Am J Gastroenterol. 2018 Jan;113(1):124-34.
[67] Stepniak D, et al. Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease. Am J Physiol Gastrointest Liver Physiol. 2006 Oct;291(4):G621-9.
[68] Salden BN, et al. Randomised clinical study: Aspergillus niger-derived enzyme digests gluten in the stomach of healthy volunteers. Aliment Pharmacol Ther. 2015 Aug;42(3):273-85.
[69] Ghoshal UC, et al. Bugs and irritable bowel syndrome: the good, the bad and the ugly. J Gastroenterol Hepatol. 2010 Feb;25(2):244-51.
[70] Oak SJ, Jha R. The effects of probiotics in lactose intolerance: a systematic review. Crit Rev Food Sci Nutr. 2019;59(11):1675-83.
[71] Sakurai T, et al. Degradation of food-derived opioid peptides by bifidobacteria. Benef Microbes. 2018 Jun 15;9(4):675-682.
[72] Dordevic D, et al. Hydrogen sulfide toxicity in the gut environment: meta-analysis of sulfate-reducing and lactic acid bacteria in inflammatory processes. J Adv Res. 2020 Mar 17;27:55-69.
The information provided is for educational purposes only. Consult your physician or healthcare provider if you have specific questions before instituting any changes in your daily lifestyle including changes in diet, exercise, and supplement use.
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Marina MacDonald, MS, PhD
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