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

Cited 5 time in scopus
Metadata Downloads
Title
Secretion of Bacillus α-amylase from yeast directed by glucoamylase I signal sequence of Saccharomyces diastaticus
Author(s)
Dae Ook Kang; In Kyu Hwang; Bo Yeon Kim; Soon Cheol Ahn; Tae Ick MheenJong Seog Ahn; Si Myung Byun
Bibliographic Citation
Biochemistry and Molecular Biology International, vol. 39, no. 1, pp. 181-190
Publication Year
1996
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
Publisher
Wiley
DOI
http://dx.doi.org/10.1080/15216549600201181
Type
Article
Appears in Collections:
Ochang Branch Institute > Chemical Biology Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.