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Title 

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

Authors 

Dae Ook KangIn Kyu HwangBo Yeon KimSoon Cheol AhnTae Ick MheenJong Seog AhnSi Myung Byun

Publisher 

International Union of Biochemistry and Molecular Biology

Issue Date 

1996

Citation 

Biochemistry and Molecular Biology International, vol. 39, no. 1, pp. 181-190

Keywords 

amylaseglucan 1,4 alpha glucosidasesignal peptidecomparative studyculture mediumescherichia coligeobacillus stearothermophilusmolecular weightpromoter regionrecombinant plasmid

Abstract 

For 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.

ISSN 

1039-9712

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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