Purification and Properties of Divalent Cation-Dependent Raw-Starch-Digesting α-Amylase from Bacillus sp. B1018

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概要

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• A raw-starch-digesting enzyme was purified to homogeneity from the culture supernatant of Bacillus sp. B1018. The molecular weight of the enzyme was about 78,000 by SDS-polyacrylamids gel electrophoresis. The temperature and pH optima were 55℃ and 5.8. The enzyme was stable up to 50℃ and at pH between 4.7 and at least 10.6. Based on the action pattern on starch, the inhibition of the activity by S-AI, and rapid depolymerization of starch, the enzyme was concluded to be an endolytic α-amylase. The K_m values of this α-amylase for hydrolysis of both raw and gelatinized starches were approximately 3 mg/ml. The saccharifying velocity of the enzyme was also essentially the same (1.7mg/ml/h) when the substrate was either raw starch or gelatinized starch. Ten mM EDTA strongly inhibited only raw starch digestion and its effect was reversed by addition of aivalent cations such as Ca^<2+> after dialysis. However, EDTA did not inhibit the adsorption of the enzyme to raw starch, so a divalent cation is necessary for the enzyme to digest raw starch, but not for the adsorption.

• 社団法人日本生物工学会の論文
• 1989-10-25

著者

• Itkor Pichet

  Department Of Food Science And Technology Faculty Of Agriculture Nagoya University

• UDAKA SHIGEZO

  Department of Fermentation Sciences, Tokyo University of Agriculture

• TSUKAGOSHI Norihiro

  Department of Food Science and Technology, Faculty of Agriculture, Nagoya University

• Udaka S

  Faculty Of Applied Bio-science Tokyo University Of Agriculture

• Udaka Shigezo

  Department Of Brewing And Fermentation Tokyo University Of Agriculture

• Udaka Shigezo

  Dept. Of Food Science And Technology Faculty Of Agriculture Nagoya University

• Tsukagoshi N

  Department Of Biological Mechanisms And Functions Graduate School Of Bioagricultural Sciences Nagoya

• Tsukagoshi Norihiro

  Department Of Applied Biological Sciences Faculty Of Agriculture Nagoya University

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