Preparation and Properties of Gelatin-Immobilized [beta]-Glucosidase from Pyrococcus furiosus
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....
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Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2005-01, Vol.69 (1), p.128 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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. |
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ISSN: | 0916-8451 1347-6947 |