SfA gene encoding α-amylase was amplified from the genomic DNA of Saccharomycopsis fibuligera CICIM Y1037 and inserted into pPIC9K,an expression vector of Pichia pastoris,to produce a recombinant pPIC9KSfA plasmid.P.pastoris GS115 was selected as an expression host.A transformant with a relatively high amylase activity was designated as P.pastoris GS115 / pPIC9K-SfA LZ08 and selected for further analysis.The molecular weight of the purified recombinant SfA was approximately 61 kDa,which was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.The optimum pH and temperature were 4.5 and 45 ℃,respectively.Therefore,SfA is possibly an acid-resistant amylase.SfA was then kept stable at 55 ℃ and pH 4.5 for 4 h in the presence of 5 mmol / L Ca2 +,and retained more than 80% of its activity.Results of high-performance liquid chromatography revealed that corn starch was hydrolyzed by SfA to form malt oligosaccharides and some glucose molecules.Maltose and maltotriose were the main products that accounted for up to 37% and 39% of the hydrolysates,respectively.Therefore,the recombinant SfA gene could be potentially applied in maltotriose and malto oligosaccharide syrup production.