Determination of glucose generation rate from various types of glycemic carbohydrates by mammalian glucosidases anchored in the small intestinal tissue
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Seo J.-M. | - |
dc.contributor.author | Lamothe L.M. | - |
dc.contributor.author | Shin H. | - |
dc.contributor.author | Austin S. | - |
dc.contributor.author | Yoo S.-H. | - |
dc.contributor.author | Lee B.-H. | - |
dc.date.available | 2020-04-06T07:38:38Z | - |
dc.date.created | 2020-04-02 | - |
dc.date.issued | 2020-07 | - |
dc.identifier.issn | 0141-8130 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/26437 | - |
dc.description.abstract | The supernatant from rat intestinal acetone powder (RIAP) was used as a source of mammalian glucosidases to determine the digestion properties of glycemic-carbohydrates. We hypothesized that many glucosidases are still anchored to the precipitated-intestinal tissues with available enzymes, and developed a method using the RIAP suspension to optimize the in vitro carbohydrate digestion model. The glucose production from various types of glycemic ingredients by RIAP suspension showed that this carbohydrate-hydrolysis model using the entire spectrum of glucosidases can be applied in an in vitro assay to determine carbohydrate quality from glycemic food products at the mammalian level. This approach better mimics the mammalian situation compared to other assays to determine the glycemic-carbohydrate digestion properties that employ fungal/microbial glucosidases that have different hydrolytic activities compared to mammalian enzymes. The method can also be used to determine the inhibitory effects of α-glucosidase inhibitors to attenuate the post-prandial blood glucose level. © 2020 Elsevier B.V. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | Elsevier B.V. | - |
dc.relation.isPartOf | International Journal of Biological Macromolecules | - |
dc.title | Determination of glucose generation rate from various types of glycemic carbohydrates by mammalian glucosidases anchored in the small intestinal tissue | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000533508600074 | - |
dc.identifier.doi | 10.1016/j.ijbiomac.2020.03.154 | - |
dc.identifier.bibliographicCitation | International Journal of Biological Macromolecules, v.154, pp.751 - 757 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.scopusid | 2-s2.0-85081973398 | - |
dc.citation.endPage | 757 | - |
dc.citation.startPage | 751 | - |
dc.citation.title | International Journal of Biological Macromolecules | - |
dc.citation.volume | 154 | - |
dc.contributor.affiliatedAuthor | Seo J.-M. | - |
dc.contributor.affiliatedAuthor | Shin H. | - |
dc.contributor.affiliatedAuthor | Lee B.-H. | - |
dc.type.docType | Article | - |
dc.subject.keywordAuthor | Carbohydrate digestion | - |
dc.subject.keywordAuthor | Glucose generation rate | - |
dc.subject.keywordAuthor | Mammalian glucosidases | - |
dc.subject.keywordPlus | acarbose | - |
dc.subject.keywordPlus | alpha glucosidase | - |
dc.subject.keywordPlus | beta galactosidase | - |
dc.subject.keywordPlus | carbohydrate | - |
dc.subject.keywordPlus | glucose | - |
dc.subject.keywordPlus | glucosidase | - |
dc.subject.keywordPlus | lactose | - |
dc.subject.keywordPlus | maltose | - |
dc.subject.keywordPlus | palatinose | - |
dc.subject.keywordPlus | sodium azide | - |
dc.subject.keywordPlus | sucrose | - |
dc.subject.keywordPlus | Article | - |
dc.subject.keywordPlus | bacterial growth | - |
dc.subject.keywordPlus | controlled study | - |
dc.subject.keywordPlus | digestion | - |
dc.subject.keywordPlus | enzyme activity | - |
dc.subject.keywordPlus | gluconeogenesis | - |
dc.subject.keywordPlus | glucose blood level | - |
dc.subject.keywordPlus | glycemic index | - |
dc.subject.keywordPlus | hydrolysis | - |
dc.subject.keywordPlus | small intestine | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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