Slowly digestible property of highly branched alpha-limit dextrins produced by 4,6-alpha-glucanotransferase from Streptococcus thermophilus evaluated in vitro and in vivo
DC Field | Value | Language |
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dc.contributor.author | Ryu, Jae-Jin | - |
dc.contributor.author | Li, Xiaolei | - |
dc.contributor.author | Lee, Eun-Sook | - |
dc.contributor.author | Li, Dan | - |
dc.contributor.author | Lee, Byung-Hoo | - |
dc.date.accessioned | 2021-10-09T03:03:14Z | - |
dc.date.available | 2021-10-09T03:03:14Z | - |
dc.date.created | 2021-10-09 | - |
dc.date.issued | 2022-01-01 | - |
dc.identifier.issn | 0144-8617 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/82339 | - |
dc.description.abstract | Starch molecules are first degraded to slowly digestible alpha-limit dextrins (alpha-LDx) and rapidly hydrolyzable linear malto-oligosaccharides (LMOs) by salivary and pancreatic alpha-amylases. In this study, we designed a slowly digestible highly branched alpha-LDx with maximized alpha-1,6 linkages using 4,6-alpha-glucanotransferase (4,6-alpha GT), which creates a short length of alpha-1,4 side chains with increasing branching points. The results showed that a short length of external chains mainly composed of 1-8 glucosyl units was newly synthesized in different amylose contents of corn starches, and the alpha-1,6 linkage ratio of branched alpha-LDx after the chromatographical purification was significantly increased from 4.6% to 22.1%. Both in vitro and in vivo studies confirmed that enzymatically modified alpha-LDx had improved slowly digestible properties and extended glycemic responses. Therefore, 4,6-alpha GT treatment enhanced the slowly digestible properties of highly branched alpha-LDx and promises usefulness as a functional ingredient to attenuate postprandial glucose homeostasis. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | ELSEVIER SCI LTD | - |
dc.relation.isPartOf | CARBOHYDRATE POLYMERS | - |
dc.title | Slowly digestible property of highly branched alpha-limit dextrins produced by 4,6-alpha-glucanotransferase from Streptococcus thermophilus evaluated in vitro and in vivo | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000701940600002 | - |
dc.identifier.doi | 10.1016/j.carbpol.2021.118685 | - |
dc.identifier.bibliographicCitation | CARBOHYDRATE POLYMERS, v.275 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.scopusid | 2-s2.0-85115773027 | - |
dc.citation.title | CARBOHYDRATE POLYMERS | - |
dc.citation.volume | 275 | - |
dc.contributor.affiliatedAuthor | Ryu, Jae-Jin | - |
dc.contributor.affiliatedAuthor | Lee, Byung-Hoo | - |
dc.type.docType | Article | - |
dc.subject.keywordAuthor | 4, 6-alpha-Glucanotransferase | - |
dc.subject.keywordAuthor | Highly branched alpha-limit dextrins | - |
dc.subject.keywordAuthor | Slow digestion | - |
dc.subject.keywordAuthor | Mammalian alpha-glucosidase | - |
dc.subject.keywordAuthor | Glycemic response | - |
dc.subject.keywordPlus | MALTASE-GLUCOAMYLASE | - |
dc.subject.keywordPlus | GLUCOSE-RELEASE | - |
dc.subject.keywordPlus | STARCH DIGESTION | - |
dc.subject.keywordPlus | ENZYME | - |
dc.subject.keywordPlus | MALTODEXTRINS | - |
dc.subject.keywordPlus | GLUCOSIDASES | - |
dc.subject.keywordPlus | AMYLOPECTIN | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | SUBSTRATE | - |
dc.subject.keywordPlus | AMYLOSE | - |
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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