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Kang, D.O. et al.

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

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.[1]

References

Secretion of Bacillus alpha-amylase from yeast directed by glucoamylase I signal sequence of Saccharomyces diastaticus. Kang, D.O., Hwang, I.K., Kim, B.Y., Ahn, S.C., Mheen, T.I., Ahn, J.S., Byun, S.M. Biochem. Mol. Biol. Int. (1996) [Pubmed]

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