Effect of phytate on the in vitro activity of digestive proteinases
Phytate inhibits the action of pepsin on the proteins but does not affect the pepsin hydrolysis of a low molecular weight substrate, acetyl-L-phenylalanyl-3,5-diioclo-L-tyrosine. The inhibition is maximal at pH 2-3 and drops to zero when the pH is increased to 4.0-4.5. Trypsin hydrolysis of both a l...
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Veröffentlicht in: | Journal of agricultural and food chemistry 1991-05, Vol.39 (5), p.859-861 |
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creator | Vaintraub, I. A Bulmaga, V. P |
description | Phytate inhibits the action of pepsin on the proteins but does not affect the pepsin hydrolysis of a low molecular weight substrate, acetyl-L-phenylalanyl-3,5-diioclo-L-tyrosine. The inhibition is maximal at pH 2-3 and drops to zero when the pH is increased to 4.0-4.5. Trypsin hydrolysis of both a low molecular weight substrate (benzoyl-D,L-arginine p-nitroanilide) and proteins is insensitive to the presence of phytate. The proteins tested include RNase and lysozyme charged positively at the pH of the trypsin hydrolysis. Thus, the inhibitory action of phytate is manifested only when it is bound with the protein substrate. The overall positive charge of protein is not a sufficient condition of phytate binding. Evidently, the protonation of protein carboxylate groups is also required |
doi_str_mv | 10.1021/jf00005a008 |
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Evidently, the protonation of protein carboxylate groups is also required</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf00005a008</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; ALBUMINAS ; ALBUMINE ; Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts ; Biological and medical sciences ; CASEINA ; CASEINE ; DIGESTIBILIDAD ; DIGESTIBILITE ; EXPERIMENTACION IN VITRO ; EXPERIMENTATION IN VITRO ; FITATOS ; Food industries ; Fundamental and applied biological sciences. 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A</creatorcontrib><creatorcontrib>Bulmaga, V. P</creatorcontrib><title>Effect of phytate on the in vitro activity of digestive proteinases</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Phytate inhibits the action of pepsin on the proteins but does not affect the pepsin hydrolysis of a low molecular weight substrate, acetyl-L-phenylalanyl-3,5-diioclo-L-tyrosine. The inhibition is maximal at pH 2-3 and drops to zero when the pH is increased to 4.0-4.5. Trypsin hydrolysis of both a low molecular weight substrate (benzoyl-D,L-arginine p-nitroanilide) and proteins is insensitive to the presence of phytate. The proteins tested include RNase and lysozyme charged positively at the pH of the trypsin hydrolysis. Thus, the inhibitory action of phytate is manifested only when it is bound with the protein substrate. The overall positive charge of protein is not a sufficient condition of phytate binding. Evidently, the protonation of protein carboxylate groups is also required</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>ALBUMINAS</subject><subject>ALBUMINE</subject><subject>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</subject><subject>Biological and medical sciences</subject><subject>CASEINA</subject><subject>CASEINE</subject><subject>DIGESTIBILIDAD</subject><subject>DIGESTIBILITE</subject><subject>EXPERIMENTACION IN VITRO</subject><subject>EXPERIMENTATION IN VITRO</subject><subject>FITATOS</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. 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P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a330t-d492eb544eca3500f6a5494ea0ef8a8b66998374aae986a22ed0cb555a4abeea3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>ALBUMINAS</topic><topic>ALBUMINE</topic><topic>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</topic><topic>Biological and medical sciences</topic><topic>CASEINA</topic><topic>CASEINE</topic><topic>DIGESTIBILIDAD</topic><topic>DIGESTIBILITE</topic><topic>EXPERIMENTACION IN VITRO</topic><topic>EXPERIMENTATION IN VITRO</topic><topic>FITATOS</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>HEMOGLOBINA</topic><topic>HEMOGLOBINE</topic><topic>HIDROLISIS</topic><topic>HYDROLYSE</topic><topic>INHIBIDORES DE ENZIMAS</topic><topic>INHIBITEUR D'ENZYME</topic><topic>PEPSINA</topic><topic>PEPSINE</topic><topic>PHYTATE</topic><topic>PROTEINAS</topic><topic>PROTEINAS VEGETALES</topic><topic>PROTEINE</topic><topic>PROTEINE VEGETALE</topic><topic>PROTEOLISIS</topic><topic>PROTEOLYSE</topic><topic>SOJA</topic><topic>TRIPSINA</topic><topic>TRYPSINE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vaintraub, I. A</creatorcontrib><creatorcontrib>Bulmaga, V. P</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vaintraub, I. A</au><au>Bulmaga, V. P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of phytate on the in vitro activity of digestive proteinases</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>1991-05-01</date><risdate>1991</risdate><volume>39</volume><issue>5</issue><spage>859</spage><epage>861</epage><pages>859-861</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>Phytate inhibits the action of pepsin on the proteins but does not affect the pepsin hydrolysis of a low molecular weight substrate, acetyl-L-phenylalanyl-3,5-diioclo-L-tyrosine. The inhibition is maximal at pH 2-3 and drops to zero when the pH is increased to 4.0-4.5. Trypsin hydrolysis of both a low molecular weight substrate (benzoyl-D,L-arginine p-nitroanilide) and proteins is insensitive to the presence of phytate. The proteins tested include RNase and lysozyme charged positively at the pH of the trypsin hydrolysis. Thus, the inhibitory action of phytate is manifested only when it is bound with the protein substrate. The overall positive charge of protein is not a sufficient condition of phytate binding. Evidently, the protonation of protein carboxylate groups is also required</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><doi>10.1021/jf00005a008</doi><tpages>3</tpages></addata></record> |
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subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ALBUMINAS ALBUMINE Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts Biological and medical sciences CASEINA CASEINE DIGESTIBILIDAD DIGESTIBILITE EXPERIMENTACION IN VITRO EXPERIMENTATION IN VITRO FITATOS Food industries Fundamental and applied biological sciences. Psychology HEMOGLOBINA HEMOGLOBINE HIDROLISIS HYDROLYSE INHIBIDORES DE ENZIMAS INHIBITEUR D'ENZYME PEPSINA PEPSINE PHYTATE PROTEINAS PROTEINAS VEGETALES PROTEINE PROTEINE VEGETALE PROTEOLISIS PROTEOLYSE SOJA TRIPSINA TRYPSINE |
title | Effect of phytate on the in vitro activity of digestive proteinases |
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