Preparation and Properties of Gelatin-Immobilized β-Glucosidase from Pyrococcus furiosus

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概要

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• Hyperthermostable β-glucosidase from Pyrococcus furiosus was enclosed in gelatin gel by cross-linking with transglutaminase. Gelatin-immobilized β-glucosidase was considerably more thermostable than the native enzyme. Lyophilized immobilisate was stored at 90 °C for 1 month without loss of activity. The immobilized β-glucosidase catalyzed transglucosylation of 5-phenylpentanol with 10.0 equivalent of cellobiose at pH 5.0 and 70 °C for 12 h to afford 5-phenylpentyl β-D-glucopyranoside in 41% yield. The immobilized enzyme was more effective than the native one in transglucosylation. The gelatin-immobilized Pfu-β-glucosidase recovered from the first run of the reaction was reusable on successive runs.

• 社団法人 日本農芸化学会の論文
• 2005-01-23

著者

• TANIGUCHI Masaki

  Hiroshima Synchrotron Radiation Center, Hiroshima University

• Sugamoto K

  Miyazaki Univ. Miyazaki Jpn

• Sugamoto Kazuhiro

  Faculty Of Engineering University Of Miyazaki

• Matsui T

  Faculty Of Engineering University Of Miyazaki

• Matsui Takanao

  Faculty Of Engineering Miyazaki University

• MATSUSHITA YOH-ICHI

  Faculty of Engineering, Miyazaki University

• NAGATOMO Hidetaka

  Faculty of Engineering, University of Miyazaki

• Sugamoto Kazuhiro

  Faculty Of Engineering Miyazaki University

• Nagatomo Hidetaka

  Faculty Of Engineering University Of Miyazaki

• Matsushita Yoh-ichi

  Faculty Of Engineering University Of Miyazaki

• Matsushita Yoh-ichi

  Faculty Of Engineering Miyazaki University

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