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Hyperthermostable -glucosidase from Pyrococcus furiosus was enclosed in gelatin gel by cross-linking with transglutaminase. Gelatin-immobilized -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 -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 -Dglucopyranoside in 41% yield. The immobilized enzyme was more effective than the native one in transglucosylation. The gelatin-immobilized Pfu--glucosidase recovered from the first run of the reaction was reusable on successive runs.