{"title":"膳食植酸造成可消化营养素损失的多样性和程度的依据:重点是鸡和猪","authors":"Edwin T. Moran, Michael R. Bedford","doi":"10.1016/j.aninu.2023.11.010","DOIUrl":null,"url":null,"abstract":"<p>Phytin is the Ca<sup>2+</sup>-Mg<sup>2+</sup>-K<sup>+</sup> salt of phytic acid that is created and deposited in the aleurone layer and/or germ of grains and legumes. Its high presence in feedstuffs for fowl and swine diets results in it being a universal and significant impediment to optimum performance. Phytin impairs gastrointestinal recovery of a wide array of nutrients, the effect varying with the nutrient concerned. On exposure to low pH during gastric digestion, phytin dissociates into phytic acid and solubilized Ca<sup>2+</sup>. Even at low gastric pH, phytic acid is negatively charged which forms the basis of its anti-nutritive behavior. Pepsinogen has extensive basic amino acids on its activation peptide that are presented as cations at low pH which are targeted by pepsin for activation. Partially crystalized Ca<sup>2+</sup> near the enzyme’s active site further stabilizes its newly formed structure. Thus, phytic acid appears to interfere with gastric digestion by several mechanisms; interfering with pepsinogen activation by binding to the polypeptide’s basic amino acids; Coordinating free Ca<sup>2+</sup>, destabilizing pepsin; binding some dietary proteins directly, further compromising gastric proteolysis. Upon digesta attaining neutrality in the duodenum, Ca<sup>2+</sup> and other cations re-bind with accessible anions, phytic acid being a significant contender. Phytate not only binds free cations but can also strip them from enzymes (e.g. Ca<sup>2+,</sup> Zn<sup>2+</sup>) which reduces their structural resistance to autolysis and ability as co-factors (e.g. Zn<sup>2+</sup>) to increase enzyme activity. Goblet cells initially employ Ca<sup>2+</sup> as an electronic shield between mucin layers enabling granule formation and cell storage. After mucin granule release, Ca<sup>2+</sup> is progressively displaced by Na<sup>+</sup> to free the viscous mucins enabling its translocation. Mucin entangles with the glycocalyx of adjacent enterocytes thereby constructing the unstirred water layer (USWL). Excessive removal of Ca<sup>2+</sup> from mucin by phytic acid increases its fluidity facilitating its loss from the USWL with its associated Na<sup>+</sup>. This partly explains increased mucin and Na<sup>+</sup> losses noted with high phytate diets. This review suggests that phytic acid binding of Ca<sup>2+</sup> and less so Zn<sup>2+</sup> is the basis for the diversity in nutrient losses encountered and that such losses are in proportion to dietary phytate content.</p>","PeriodicalId":8184,"journal":{"name":"Animal Nutrition","volume":"6 1","pages":""},"PeriodicalIF":6.1000,"publicationDate":"2024-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Basis for the diversity and extent in loss of digestible nutrients created by dietary phytin: Emphasis on fowl and swine\",\"authors\":\"Edwin T. Moran, Michael R. Bedford\",\"doi\":\"10.1016/j.aninu.2023.11.010\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>Phytin is the Ca<sup>2+</sup>-Mg<sup>2+</sup>-K<sup>+</sup> salt of phytic acid that is created and deposited in the aleurone layer and/or germ of grains and legumes. Its high presence in feedstuffs for fowl and swine diets results in it being a universal and significant impediment to optimum performance. Phytin impairs gastrointestinal recovery of a wide array of nutrients, the effect varying with the nutrient concerned. On exposure to low pH during gastric digestion, phytin dissociates into phytic acid and solubilized Ca<sup>2+</sup>. Even at low gastric pH, phytic acid is negatively charged which forms the basis of its anti-nutritive behavior. Pepsinogen has extensive basic amino acids on its activation peptide that are presented as cations at low pH which are targeted by pepsin for activation. Partially crystalized Ca<sup>2+</sup> near the enzyme’s active site further stabilizes its newly formed structure. Thus, phytic acid appears to interfere with gastric digestion by several mechanisms; interfering with pepsinogen activation by binding to the polypeptide’s basic amino acids; Coordinating free Ca<sup>2+</sup>, destabilizing pepsin; binding some dietary proteins directly, further compromising gastric proteolysis. Upon digesta attaining neutrality in the duodenum, Ca<sup>2+</sup> and other cations re-bind with accessible anions, phytic acid being a significant contender. Phytate not only binds free cations but can also strip them from enzymes (e.g. Ca<sup>2+,</sup> Zn<sup>2+</sup>) which reduces their structural resistance to autolysis and ability as co-factors (e.g. Zn<sup>2+</sup>) to increase enzyme activity. Goblet cells initially employ Ca<sup>2+</sup> as an electronic shield between mucin layers enabling granule formation and cell storage. After mucin granule release, Ca<sup>2+</sup> is progressively displaced by Na<sup>+</sup> to free the viscous mucins enabling its translocation. Mucin entangles with the glycocalyx of adjacent enterocytes thereby constructing the unstirred water layer (USWL). Excessive removal of Ca<sup>2+</sup> from mucin by phytic acid increases its fluidity facilitating its loss from the USWL with its associated Na<sup>+</sup>. This partly explains increased mucin and Na<sup>+</sup> losses noted with high phytate diets. This review suggests that phytic acid binding of Ca<sup>2+</sup> and less so Zn<sup>2+</sup> is the basis for the diversity in nutrient losses encountered and that such losses are in proportion to dietary phytate content.</p>\",\"PeriodicalId\":8184,\"journal\":{\"name\":\"Animal Nutrition\",\"volume\":\"6 1\",\"pages\":\"\"},\"PeriodicalIF\":6.1000,\"publicationDate\":\"2024-01-08\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Animal Nutrition\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://doi.org/10.1016/j.aninu.2023.11.010\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"AGRICULTURE, DAIRY & ANIMAL SCIENCE\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Animal Nutrition","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1016/j.aninu.2023.11.010","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, DAIRY & ANIMAL SCIENCE","Score":null,"Total":0}
Basis for the diversity and extent in loss of digestible nutrients created by dietary phytin: Emphasis on fowl and swine
Phytin is the Ca2+-Mg2+-K+ salt of phytic acid that is created and deposited in the aleurone layer and/or germ of grains and legumes. Its high presence in feedstuffs for fowl and swine diets results in it being a universal and significant impediment to optimum performance. Phytin impairs gastrointestinal recovery of a wide array of nutrients, the effect varying with the nutrient concerned. On exposure to low pH during gastric digestion, phytin dissociates into phytic acid and solubilized Ca2+. Even at low gastric pH, phytic acid is negatively charged which forms the basis of its anti-nutritive behavior. Pepsinogen has extensive basic amino acids on its activation peptide that are presented as cations at low pH which are targeted by pepsin for activation. Partially crystalized Ca2+ near the enzyme’s active site further stabilizes its newly formed structure. Thus, phytic acid appears to interfere with gastric digestion by several mechanisms; interfering with pepsinogen activation by binding to the polypeptide’s basic amino acids; Coordinating free Ca2+, destabilizing pepsin; binding some dietary proteins directly, further compromising gastric proteolysis. Upon digesta attaining neutrality in the duodenum, Ca2+ and other cations re-bind with accessible anions, phytic acid being a significant contender. Phytate not only binds free cations but can also strip them from enzymes (e.g. Ca2+, Zn2+) which reduces their structural resistance to autolysis and ability as co-factors (e.g. Zn2+) to increase enzyme activity. Goblet cells initially employ Ca2+ as an electronic shield between mucin layers enabling granule formation and cell storage. After mucin granule release, Ca2+ is progressively displaced by Na+ to free the viscous mucins enabling its translocation. Mucin entangles with the glycocalyx of adjacent enterocytes thereby constructing the unstirred water layer (USWL). Excessive removal of Ca2+ from mucin by phytic acid increases its fluidity facilitating its loss from the USWL with its associated Na+. This partly explains increased mucin and Na+ losses noted with high phytate diets. This review suggests that phytic acid binding of Ca2+ and less so Zn2+ is the basis for the diversity in nutrient losses encountered and that such losses are in proportion to dietary phytate content.
Animal NutritionAgricultural and Biological Sciences-Animal Science and Zoology
CiteScore
7.40
自引率
3.20%
发文量
172
审稿时长
12 weeks
期刊介绍:
Animal Nutrition encompasses the full gamut of animal nutritional sciences and reviews including, but not limited to, fundamental aspects of animal nutrition such as nutritional requirements, metabolic studies, body composition, energetics, immunology, neuroscience, microbiology, genetics and molecular and cell biology related to nutrition, and more applied aspects of animal nutrition, such as raw material evaluation, feed additives, nutritive value of novel ingredients and feed safety.