Baeva L F, Kozlov D G, Brevnova E E, Benevolenskiĭ S V
Prikl Biokhim Mikrobiol. 1996 May-Jun;32(3):311-4.
The alpha-amylase gene of yeast Saccharomycopsis fibuligera was cloned, partially sequenced, and expressed in Saccharomyces cerevisiae. Four amino acid substitutions were identified in the enzyme structure as compared to the earlier cloned gene. The Saccharomycopsis fibuligera alpha-amylase gene was expressed in Saccharomyces cerevisiae under the control of its own promoter. The native alpha-amylase signal peptide provided an efficient secretion of the enzyme by Saccharomyces cerevisiae. The efficiency of the alpha-amylase secretion was 98%. The pH optimum of the enzyme secreted by Saccharomyces cerevisiae was 4.0.
扣囊复膜孢酵母的α-淀粉酶基因被克隆、部分测序，并在酿酒酵母中表达。与早期克隆的基因相比，在该酶结构中鉴定出四个氨基酸取代。扣囊复膜孢酵母α-淀粉酶基因在其自身启动子的控制下在酿酒酵母中表达。天然α-淀粉酶信号肽可使酿酒酵母高效分泌该酶。α-淀粉酶的分泌效率为98%。酿酒酵母分泌的该酶的最适pH为4.0。
