Number of branch points in alpha-limit dextrins impact glucose generation rates by mammalian mucosal alpha-glucosidases
DC Field | Value | Language |
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dc.contributor.author | Lee, Byung-Hoo | - |
dc.contributor.author | Hamaker, Bruce R. | - |
dc.date.available | 2020-02-27T19:43:36Z | - |
dc.date.created | 2020-02-07 | - |
dc.date.issued | 2017-02-10 | - |
dc.identifier.issn | 0144-8617 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/6400 | - |
dc.description.abstract | alpha-Amylase first hydrolyzes starch structures to linear maltooligosaccharides and branched alpha-limit dextrins, then complete hydrolysis to glucose takes place through the mucosal alpha-glucosidases. In this study, we hydrolyzed waxy corn starch (WCS) by human pancreatic alpha-amylase to determine the digestion and structural properties of different size fractions of the branched alpha-limit dextrins. The alpha-amylolyzed WCS was separated by size exclusion chromatography, and the analyzed chromatograms showed four main hydrolyzate fractions. The first three eluted peaks (regions I-III) corresponded to branched alpha-limit dextrins, while region IV was the linear maltooligosaccharides. Based on the chromatographic and NMR analyses of the individual peaks, Region I, II, and III had multiple (>2), two, and one alpha-1,6 linkages, respectively, and region I was the most slowly hydrolyzed to glucose by mucosal alpha-glucosidases (hydrolysis rate: Region I < II < III < IV). This study shows the possibility of producing slowly digestible oligosaccharides that may decrease postprandial glycemic response and control glucose delivery to the body, to address metabolic syndrome-associated diseases. (C) 2016 Published by Elsevier Ltd. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | ELSEVIER SCI LTD | - |
dc.relation.isPartOf | CARBOHYDRATE POLYMERS | - |
dc.subject | MALTASE-GLUCOAMYLASE ACTIVITY | - |
dc.subject | SUCRASE-ISOMALTASE | - |
dc.subject | STARCH DIGESTION | - |
dc.subject | GLYCEMIC INDEX | - |
dc.subject | SUBSTRATE BRAKE | - |
dc.subject | SPECIFICITY | - |
dc.subject | HEALTH | - |
dc.subject | ENZYME | - |
dc.subject | 4-ALPHA-GLUCANOTRANSFERASE | - |
dc.subject | CLASSIFICATION | - |
dc.title | Number of branch points in alpha-limit dextrins impact glucose generation rates by mammalian mucosal alpha-glucosidases | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000391896800024 | - |
dc.identifier.doi | 10.1016/j.carbpol.2016.09.088 | - |
dc.identifier.bibliographicCitation | CARBOHYDRATE POLYMERS, v.157, pp.207 - 213 | - |
dc.identifier.scopusid | 2-s2.0-84988955576 | - |
dc.citation.endPage | 213 | - |
dc.citation.startPage | 207 | - |
dc.citation.title | CARBOHYDRATE POLYMERS | - |
dc.citation.volume | 157 | - |
dc.contributor.affiliatedAuthor | Lee, Byung-Hoo | - |
dc.type.docType | Article | - |
dc.subject.keywordAuthor | alpha-limit dextrins | - |
dc.subject.keywordAuthor | Starch | - |
dc.subject.keywordAuthor | Slow digestion | - |
dc.subject.keywordAuthor | alpha-glucosidases Human | - |
dc.subject.keywordAuthor | alpha-amylase | - |
dc.subject.keywordPlus | MALTASE-GLUCOAMYLASE ACTIVITY | - |
dc.subject.keywordPlus | SUCRASE-ISOMALTASE | - |
dc.subject.keywordPlus | STARCH DIGESTION | - |
dc.subject.keywordPlus | GLYCEMIC INDEX | - |
dc.subject.keywordPlus | SUBSTRATE BRAKE | - |
dc.subject.keywordPlus | SPECIFICITY | - |
dc.subject.keywordPlus | HEALTH | - |
dc.subject.keywordPlus | ENZYME | - |
dc.subject.keywordPlus | 4-ALPHA-GLUCANOTRANSFERASE | - |
dc.subject.keywordPlus | CLASSIFICATION | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalResearchArea | Polymer Science | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Applied | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Organic | - |
dc.relation.journalWebOfScienceCategory | Polymer Science | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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