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Antioxidant and ACE inhibitory activities of soybean hydrolysates: Effect of enzyme and degree of hydrolysis

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dc.contributor.authorLee, Ji-Soo-
dc.contributor.authorYoo, Mi Ae-
dc.contributor.authorKoo, Seung Hlyun-
dc.contributor.authorBaek, Hyung-Hee-
dc.contributor.authorLee, Hyeon Gyu-
dc.date.accessioned2022-10-07T10:08:07Z-
dc.date.available2022-10-07T10:08:07Z-
dc.date.created2022-08-26-
dc.date.issued2008-08-
dc.identifier.issn1226-7708-
dc.identifier.urihttps://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/171908-
dc.description.abstractNative soy protein isolate (SPI) was hydrolyzed with 4 different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the degree of hydrolysis (DH) in range of 6 to 15% were prepared by each enzyme. The angiotensin I converting enzyme (ACE) inhibitory and the antioxidant activities of the SPI hydrolysates, such as superoxide dismutase-like activity and inhibition of the linoleic acid autoxidation, were evaluated. Overall, as the DH increased, all evaluated bioactivities of the SPI hydrolysates significantly increased. The significantly highest ACE inhibitory and antioxidant activities were found in hydrolysates made with papain and bromelain, respectively. SPI hydrolysates by Flavourzyme showed the significantly lowest activity in all tested bioactivities. The results suggested that ACE inhibitory and antioxidant activities of SPI hydrolysates were determined by the DH and by the enzyme used.-
dc.language영어-
dc.language.isoen-
dc.publisherKOREAN SOC FOOD SCIENCE TECHNOLOGY-
dc.titleAntioxidant and ACE inhibitory activities of soybean hydrolysates: Effect of enzyme and degree of hydrolysis-
dc.typeArticle-
dc.contributor.affiliatedAuthorLee, Hyeon Gyu-
dc.identifier.scopusid2-s2.0-56349091423-
dc.identifier.wosid000258870200036-
dc.identifier.bibliographicCitationFOOD SCIENCE AND BIOTECHNOLOGY, v.17, no.4, pp.873 - 877-
dc.relation.isPartOfFOOD SCIENCE AND BIOTECHNOLOGY-
dc.citation.titleFOOD SCIENCE AND BIOTECHNOLOGY-
dc.citation.volume17-
dc.citation.number4-
dc.citation.startPage873-
dc.citation.endPage877-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.identifier.kciidART001272049-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.description.journalRegisteredClasskci-
dc.relation.journalResearchAreaFood Science & Technology-
dc.relation.journalWebOfScienceCategoryFood Science & Technology-
dc.subject.keywordPlusANGIOTENSIN-CONVERTING ENZYME-
dc.subject.keywordPlusPROTEIN HYDROLYSATE-
dc.subject.keywordPlusBIOACTIVE PEPTIDES-
dc.subject.keywordPlusFUNCTIONAL-PROPERTIES-
dc.subject.keywordPlusMILK-PROTEINS-
dc.subject.keywordPlusSOY-
dc.subject.keywordPlusACID-
dc.subject.keywordPlusFOOD-
dc.subject.keywordPlusHISTIDINE-
dc.subject.keywordPlusASSAY-
dc.subject.keywordAuthorsoy protein isolate-
dc.subject.keywordAuthorangiotensin I converting enzyme (ACE) inhibitory activity-
dc.subject.keywordAuthorantioxidant activity-
dc.subject.keywordAuthordegree of hydrolysis-
dc.subject.keywordAuthorproteolytic enzyme-
dc.identifier.urlhttps://scienceon.kisti.re.kr/srch/selectPORSrchArticle.do?cn=JAKO200833338360909&SITE=CLICK-
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