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Comparative Study
. 1996 May;39(1):181-90.
doi: 10.1080/15216549600201181.

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

D O Kang  1 , I K Hwang, B Y Kim, S C Ahn, T I Mheen, J S Ahn, S M Byun
Affiliations
Comparative Study

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

D O Kang et al. Biochem Mol Biol Int. 1996 May.

Abstract

For the secretion of Bacillus stearothermophilus alpha-amylase from yeast, a recombinant plasmid pGAT17 was constructed by fusing B. stearothermophilus alpha-amylase structural gene in frame to the promoter and signal sequence of Saccharomyces diastaticus glucoamylase I gene (STA1). The secretion of the heterologous alpha-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 alpha-amylase activity was detected in the extracellular culture medium. The secreted alpha-amylase was glycosylated and its molecular weight increased from 61 kDa to 75 kDa. The thermostability of the the glycosylated alpha-amylase was markedly enhanced, compared with that of the non-glycosylated enzyme from E. coli.

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