Different inhibition properties of catechins on the individual subunits of mucosal alpha-glucosidases as measured by partially-purified rat intestinal extract
DC Field | Value | Language |
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dc.contributor.author | Lim, Jongbin | - |
dc.contributor.author | Kim, Do Kyoung | - |
dc.contributor.author | Shin, Hansol | - |
dc.contributor.author | Hamaker, Bruce R. | - |
dc.contributor.author | Lee, Byung-Hoo | - |
dc.date.available | 2020-02-27T02:41:37Z | - |
dc.date.created | 2020-02-04 | - |
dc.date.issued | 2019-07-01 | - |
dc.identifier.issn | 2042-6496 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/1255 | - |
dc.description.abstract | Mucosal alpha-glucosidases from rat intestinal powder were employed, with a step to remove alpha-amylase, to measure the possibility of different inhibition of catechins, particularly those found in tea, on the four alpha-glucosidase enzymes. Inhibition of catechins was investigated for the slowing of digestion of glycemic carbohydrates, thus regulating glucose release and absorption. The alpha-glucosidases were fractionated using size-exclusion chromatography. The partially purified fractions showed higher alpha-glucosidase activity without any alpha-amylase activity. Catechins had selective inhibition properties on the alpha-glucosidases. In particular, (-)-epigallocatechin gallate (EGCG) and (-)-epicatechin gallate (ECG) showed comparably high inhibitory effect on all four individual alpha-glucosidases, while (-)-epicatechin (EC), and (+)-catechin (C) indicated a more discriminating effect with relatively higher inhibitory effects on sucrase-isomaltase. The findings suggest that catechins differently inhibit the individual subunits of the alpha-glucosidases, and that they could modulate postprandial blood glucose levels through slowing digestion rate of starch and other glycemic carbohydrates, including sucrose. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | ROYAL SOC CHEMISTRY | - |
dc.relation.isPartOf | FOOD & FUNCTION | - |
dc.subject | DIGESTING MALTASE-GLUCOAMYLASE | - |
dc.subject | SUCRASE-ISOMALTASE | - |
dc.subject | STARCH DIGESTION | - |
dc.subject | EPIGALLOCATECHIN GALLATE | - |
dc.subject | ENZYME SPECIFICITIES | - |
dc.subject | PHENOLIC-COMPOUNDS | - |
dc.subject | TEA POLYPHENOLS | - |
dc.subject | ACTION PATTERN | - |
dc.subject | AMYLASE | - |
dc.subject | ACARBOSE | - |
dc.title | Different inhibition properties of catechins on the individual subunits of mucosal alpha-glucosidases as measured by partially-purified rat intestinal extract | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000476683600051 | - |
dc.identifier.doi | 10.1039/c9fo00990f | - |
dc.identifier.bibliographicCitation | FOOD & FUNCTION, v.10, no.7, pp.4407 - 4413 | - |
dc.identifier.scopusid | 2-s2.0-85069543276 | - |
dc.citation.endPage | 4413 | - |
dc.citation.startPage | 4407 | - |
dc.citation.title | FOOD & FUNCTION | - |
dc.citation.volume | 10 | - |
dc.citation.number | 7 | - |
dc.contributor.affiliatedAuthor | Kim, Do Kyoung | - |
dc.contributor.affiliatedAuthor | Shin, Hansol | - |
dc.contributor.affiliatedAuthor | Lee, Byung-Hoo | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | DIGESTING MALTASE-GLUCOAMYLASE | - |
dc.subject.keywordPlus | SUCRASE-ISOMALTASE | - |
dc.subject.keywordPlus | STARCH DIGESTION | - |
dc.subject.keywordPlus | EPIGALLOCATECHIN GALLATE | - |
dc.subject.keywordPlus | ENZYME SPECIFICITIES | - |
dc.subject.keywordPlus | PHENOLIC-COMPOUNDS | - |
dc.subject.keywordPlus | TEA POLYPHENOLS | - |
dc.subject.keywordPlus | ACTION PATTERN | - |
dc.subject.keywordPlus | AMYLASE | - |
dc.subject.keywordPlus | ACARBOSE | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Food Science & Technology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Food Science & Technology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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