Purification and Substrate Specificity of α-Glucosidase from Paecilomyces varioti AHU 9417

概要

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An extracellular α-glucosidase was purified from the culture broth of Paecilomyces varioti AHU 9417 by a combination of precipitation with ethanol, chromatography on DEAE-Sepharose CL-6B and Bio-Gel P-150,and preparative gel electrophoresis. The enzyme migrated as a single band on polyacrylamide gel electrophoresis. The molecular weight was estimated to be 100,000 by SDS-disc electrophoresis, and the optimum pH of activity was 4.5. The enzyme had a wide substrate specificity, as it rapidly hydrolyzed maltooligosaccharides and isomaltooligosaccharides. The ratios of V_<max> for maltose, isomaltose, kojibiose, nigerose, phenyl α-glucoside, maltotriose, isomaltotriose, panose, phenyl α-maltoside, and soluble starch were estimated to be 100,72,31,105,9.6,103,73,47,115,and 66,and the K_m (mM of nonreducing terminal) for these substrates were 0.40,2.4,1.6,2.5,0.23,0.33,4.6,0.67,0.24,and 4.7 mM, respectively. The enzyme is characterized by a high activity toward isomaltose.
社団法人日本農芸化学会の論文
1992-12-23