“Abstract: Food allergy prevalence numbers are still on the rise. Apart from environmental in\ufb02uences, dietary habits, food availability and life-style factors, medication could also play a role. For immune tolerance of food, several contributing factors ensure that dietary compounds are immunologically ignored and serve only as source for energy and nutrient supply. Functional digestion along the gastrointestinal tract is essential for the molecular breakdown and a prerequisite for appropriate uptake in the intestine. Digestion and digestibility of carbohydrates and proteins thus critically affect the risk of food allergy development. In this review, we highlight the in\ufb02uence of amylases, gastric acid- and trypsin-inhibitors, as well as of food processing in the context of food allergenicity.
\nOmissis\u2026..Furthermore, digestion and digestibility could determine whether food proteins are tolerated or become sensitizing agents. This aspect has therefore even been taken up by the European Food Safety Agency in their scienti\ufb01c opinion about evaluation of allergenicity of food and feed proteins. Higher resistance to digestion or survival along the digestive tract seems to increase the sensitization capacity of a food component and renders it more immunogenic and\/or allergenic. Based on this scienti\ufb01c background, the present review article highlights factors in\ufb02uencing protein digestion and digestibility.<\/p>\n
From the study:<\/p>\n
Digestion of Carbohydrates: Amylase Action Critical for Starch Digestion and Microbiome<\/strong><\/p>\n \u2026\u2026..Omissis. Starch is digested by speci\ufb01c enzymes, i.e., amylases, which cleave the \u03b1-1,4-glucosidic bond of its major compound amylose, as well as the \u03b1-1,6-glucosidic bond of the second major constituent, amylopectin [15].<\/p>\n \u2026.. Omissis. In humans, \u03b1-amylase is a product of the exocrine pancreas. Animal models suggest that microbial amylases could be supplied in pancreas insuf\ufb01ciency [18]. It is not known whether this will be linked to a risk for sensitization, but \u03b1-amylase per se when inhaled is a well-known occupational allergen. In baker\u2019s asthma associated with the \ufb02our processing industry, allergenic amylase derives from contaminating fungi [19]. In mammals, amylase is also secreted into the saliva. Its role in starch digestion has been questioned due to its low amount relative to the overall amylase activity [20]. However, in vitro studies strongly propose that salivary amylolytic activity hydrolyzes up to 80% of bread starch in the \ufb01rst 30 min of gastric digestion, independent of acidi\ufb01cation by the gastric juices [21]. This critically affects the quality of remnants reaching the intestine, which will affect the composition of the micro\ufb02ora (discussed below).<\/p>\n \u2026\u2026…Omissis. The amylase action on rapidly digestible starch (RDS) renders smaller products, like disaccharides and trisaccharides [25]. These are then further hydrolyzed to glucose by other enzymes, such as \u03b1-glucosidase in the small intestine [26]. However, both amylase and \u03b1-glucosidase may act synergistically. Some compounds represent slow-digestible starch (SDS), or resistant starch (RS) as larger leftovers, which persist the gastrointestinal transit to a large degree. Usually, resulting levels of malto-oligosaccharide indicate the degree of granular starch breakdown. The starch breakdown by amylases is largely in\ufb02uenced by the composition of the food processing and matrix composition. Cooking has been shown to enhance the amylase breakdown of starch [27], which also depended on the individual \u03b1-amylase activity. Flavonoids are important plant constituents, which interfere with amylase activity by hydrophobic interaction in the food matrix or by formation of covalent bonds during cooking or in gastric juice, and therefore impair starch digestion [28]. This opens up potential intervention strategies in diabetic patients to decrease the fermentation speed of starch and thereby inhibit an undesired fast release of glucose. Starch may also form complexes with lipids in the food matrix, e.g., complex formation with palm oil interfered with the digestion of rice starches [29]. Interestingly, some fresh food may neutralize amylases by proteolysis. Kiwi contains actinidin, a cysteine proteinase, which speci\ufb01cally attacks amylase and thereby may inhibit starch digestion [30]. This may affect the presentation of allergenic epitopes in the food matrix. Amylase in the duodenum also plays a key role in the breakdown of gluten and may therefore modulate its pathophysiologic role in celiac disease [31]. While starch forms complexes with gluten during baking of bread, amylase resolves them and makes gluten accessible for thorough protein digestion. Wheat on the other hand contains anti-enzymes, such as the ATIs (amylase-trypsin inhibitors) with a role in non-celiac gluten sensitivity (NCGS) [32]. Nutritional ATIs additionally stimulate the innate immune reaction via TLR4 [32] and thereby exacerbate allergic in\ufb02ammation not only in the intestine, but also in the airways in mouse models [33,34]. It is hypothesized that industrial food processing contributes to the increased numbers of non-celiac gluten\/wheat sensitivity by stabilizing e.g., starch-gluten complexes, thereby bypassing the salivary and pancreatic enzymes, leaving the digestion to mucosal amylases [35]”. \u201cThe Effect of Digestion and Digestibility on Allergenicity of Food Isabella Pali-Scholl, Eva Untersmayr, Martina Klems and Erika Jensen-Jarolim. Published: 21 August 2018 Nutrients.\u201d<\/p>\n","protected":false},"excerpt":{"rendered":" “Abstract: Food allergy prevalence numbers are still on the rise. Apart from environmental in\ufb02uences, dietary habits, food availability and life-style factors, medication could also play a role. For immune tolerance of food, several contributing factors ensure that dietary compounds are immunologically ignored and serve only as source for energy and nutrient supply. Functional digestion along […]<\/p>\n","protected":false},"author":2,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[73],"tags":[987],"class_list":["post-1718","post","type-post","status-publish","format-standard","hentry","category-article","tag-anti-acid-acid-suppressing-medication-blocked-digestion-food-allergy-gastritis-impaired-digestion-maillard-reux-ulcer"],"yoast_head":"\n