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A very efficient beta-glucosidase catalyst for the hydrolysis of flavor precursors of wines and fruit juices

Gueguen, Y., Chemardin, P., Janbon, G., Arnaud, A., Galzy, P.
Journal of agricultural and food chemistry 1996 v.44 no.8 pp. 2336-2340
wines, fruit juices, flavor compounds, odors, beta-glucosidase, enzyme activity, physicochemical properties
Candida molischiana 35M5N beta-glucosidase was immobilized to Duolite A-568 resin. Higher immobilization efficiency (86%) was achieved with citrate-phosphate buffer (0.1 M) at pH 4. The study of the immobilized beta-glucosidase demonstrated that the physicochemical properties were similar to those of the free enzyme. Free and immobilized beta-glucosidase were used to treat muscat wine and apricot fruit juice. GC-MS analysis indicated a significant increase in the flavor compounds nerol, geraniol, linalool, 2-phenylethanol, and benzyl alcohol in the muscat wine and linalool, alpha- and gamma-terpinene, alpha-terpineol, 2-phenylethanol, and alpha-pinene in the apricot fruit juice. The immobilized beta-glucosidase was found to be very stable under fruit juice or wine conditions and could be used repeatedly for several hydrolyses of bound aroma. The efficiency of this experimental catalyst was successfully tested with several fruit juices and wines containing various amounts of precursors.