Purification and Characterization of β-Amylase from Bacillus cereus BQ10-S1 Spo II

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概要

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• β-Amylase produced by Bacillus cereus BQ10-S1 Spo II was purified by salting out with ammoniumsulfate, and column chromatography on Sephadex G-100 and CM-SephadexC-50. The purified enzyme was homogeneouson disc electrophoresis and ultracentrifugation. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of the enzymeshowed a single band suggesting no subunit structure. The sedimentation coefficient was 4.8S20, w and the molecular weight was estimated to be 6.0×104 by SDS-PAGE, 6.2×104 by gel filtration in the presence of6m guanidine HCl, 6.25×104 by sedimentation equilibrium and 5.5×104 by amino acid analysis, respectively. The Kmvalue for soluble starch was 0.4%. The enzyme was remarkably inhibited by 5×10-9m PCMBbut not by DTNBat the same concentration. Only one sulfhydryl group was detected by amino acid analysis, by Ellumans and Riordans methods. The isoelectric point of the purified enzyme was 8.3.

• 社団法人 日本農芸化学会の論文

著者

• Shinke Ryu

  Department Of Agricultural Chemistry Faculty Of Agriculture Kobe University

• Nanmori Takashi

  Department Of Agricultural Chemistry Faculty Of Agriculture Kobe University

• Aoki Kenji

  Department Of Agricultural Chemistry Faculty Of Agriculture Kobe University

• Nishira Hiroshi

  Department Of Agricultural Chemistry Faculty Of Agriculture Kobe University

• NANMORI Takashi

  Department of Utilization of Biological Resources, Division of Science of Biological Resources, Graduate School of Science and Technology

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