Secretion of Bacillus α-amylase from yeast directed by glucoamylase I signal sequence of Saccharomyces diastaticus

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dc.contributor.authorDae Ook Kang-
dc.contributor.authorIn Kyu Hwang-
dc.contributor.authorBo Yeon Kim-
dc.contributor.authorSoon Cheol Ahn-
dc.contributor.authorTae Ick Mheen-
dc.contributor.authorJong Seog Ahn-
dc.contributor.authorSi Myung Byun-
dc.date.accessioned2017-04-19T08:45:28Z-
dc.date.available2017-04-19T08:45:28Z-
dc.date.issued1996-
dc.identifier.issn1039-9712-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/3753-
dc.description.abstractFor the secretion of Bacillus stearothermophilus α-amylase from yeast, a recombinant plasmid pGAT17 was constructed by fusing B. stearothermophilus a -amylase structural gene in frame to the promoter and signal sequence of Saccharomyces diastaticus glucoamylase I gene (STA1). The secretion of the heterologous α-amylase from S. diastaticus transformed with pGAT17 was confirmed by the halo formation around colonies on selective starch agar medium. About 80% of the total α-amylase activity was detected in the extracellular culture medium. The secreted α-amylase was glycosylated and its molecular weight increased from 61 kDa to 75 kDa. The thermostability of the the glycosylated a -amylase was markedly enhanced, compared with that of the non-glycosylated enzyme from E. coli.-
dc.publisherWiley-
dc.titleSecretion of Bacillus α-amylase from yeast directed by glucoamylase I signal sequence of Saccharomyces diastaticus-
dc.title.alternativeSecretion of Bacillus α-amylase from yeast directed by glucoamylase I signal sequence of Saccharomyces diastaticus-
dc.typeArticle-
dc.citation.titleBiochemistry and Molecular Biology International-
dc.citation.number1-
dc.citation.endPage190-
dc.citation.startPage181-
dc.citation.volume39-
dc.contributor.affiliatedAuthorDae Ook Kang-
dc.contributor.affiliatedAuthorBo Yeon Kim-
dc.contributor.affiliatedAuthorSoon Cheol Ahn-
dc.contributor.affiliatedAuthorTae Ick Mheen-
dc.contributor.affiliatedAuthorJong Seog Ahn-
dc.contributor.alternativeName강대욱-
dc.contributor.alternativeName황인규-
dc.contributor.alternativeName김보연-
dc.contributor.alternativeName안순철-
dc.contributor.alternativeName민태익-
dc.contributor.alternativeName안종석-
dc.contributor.alternativeName변시명-
dc.identifier.bibliographicCitationBiochemistry and Molecular Biology International, vol. 39, no. 1, pp. 181-190-
dc.identifier.doi10.1080/15216549600201181-
dc.description.journalClassY-
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Ochang Branch Institute > Chemical Biology Research Center > 1. Journal Articles
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