Purification and Characterization of Acid α-Amylase from Paecilomyces sp.

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This paper deals with purification and characterization of Paecilomyces α-amylase. Crude enzyme prepared by solid fermentation was further purified by fraction with ammonium sulfate, DEAE-cellulose column chromatography, CM-cellulose chromatography, and Sephadex G-200 gel filtration. The purified enzyme was electrophoretically homogeneous and optimally hydrolyzed starch at pH 4,which is a lower pH optimum compared to other α-amylases. The optimum temperature was 45℃, and the enzyme was stable between pH 4-9. The molecular weight of the enzyme was 69,000. It was also found that Ca^<2+> plays an important role in the enzyme stability. Paper chromatography demonstrated that the α-amylase produced significant amounts of glucose and maltoriose with lower amounts of maltose and other oligosaccharides. The chromatographic pattern of the Paecilomyces enzyme is quite different to those of enzymes from Bacillus subtilis, B. polymyxa, and Aspergillus oryzae.
公益社団法人日本生物工学会の論文
1983-02-25