Effect of chloride ions on the catalytic properties of human pancreatic a-amylase isozyme produced in Pichia pastoris
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, M.-G. | - |
dc.contributor.author | Kim, Y.-W. | - |
dc.date.accessioned | 2021-09-04T08:51:55Z | - |
dc.date.available | 2021-09-04T08:51:55Z | - |
dc.date.created | 2021-06-17 | - |
dc.date.issued | 2016 | - |
dc.identifier.issn | 0367-6293 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/91392 | - |
dc.description.abstract | The AMY2B gene, encoding human pancreatic a-amylase isozyme (HPA II), was expressed in Pichia pastoris, and the effects of chloride ions on HPA II activity toward starch substrates were investigated. As seen with chloride ion-dependent a-amylases-including HPA I, the isozyme of HPA II-chloride ions increased enzyme activity and shifted the optimal pH to an alkaline pH. The activity enhancement by chloride was more significant at pH 8 than that at pH 6, suggesting that the protonation state of the general acid/base catalyst of HPA II was important for the hydrolysis of starches at an alkaline pH because of the increase in its pKa by chloride ions. The turnover values for cereal starches as the substrates markedly increased in the presence of chloride by up to 7.2-fold, whereas that for soluble starch increased by only 1.7-fold. Chloride inhibited substrate hydrolysis at high substrate concentrations, with Ki values ranging from 6 to 15 mg/mL. © The Korean Society of Food Science and Technology. | - |
dc.language | Korean | - |
dc.language.iso | ko | - |
dc.publisher | Korean Society of Food Science and Technology | - |
dc.title | Effect of chloride ions on the catalytic properties of human pancreatic a-amylase isozyme produced in Pichia pastoris | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Y.-W. | - |
dc.identifier.doi | 10.9721/KJFST.2016.48.4.341 | - |
dc.identifier.scopusid | 2-s2.0-84989234987 | - |
dc.identifier.bibliographicCitation | Korean Journal of Food Science and Technology, v.48, no.4, pp.341 - 346 | - |
dc.relation.isPartOf | Korean Journal of Food Science and Technology | - |
dc.citation.title | Korean Journal of Food Science and Technology | - |
dc.citation.volume | 48 | - |
dc.citation.number | 4 | - |
dc.citation.startPage | 341 | - |
dc.citation.endPage | 346 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.identifier.kciid | ART002141344 | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.subject.keywordAuthor | Chloride ion | - |
dc.subject.keywordAuthor | Human pancreatic a-amylase | - |
dc.subject.keywordAuthor | Isozyme | - |
dc.subject.keywordAuthor | Kinetics | - |
dc.subject.keywordAuthor | Substrate inhibition | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
(02841) 서울특별시 성북구 안암로 14502-3290-1114
COPYRIGHT © 2021 Korea University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.