A thermostable β-glucosidase was effectively immobilized on alginate by the method of gel entrapment. After optimization of immobilized conditions, recovered enzyme activity was 60%. Optimum pH, temperature, kinetic parameters, thermal and pH stability, reusability, and storage stability were investigated. The and for immobilized β-glucosidase were estimated to be 5.0？mM and 0.64？U/ml, respectively. When comparing, free and immobilized enzyme, change was observed in optimum pH and temperature from 5.0 to 6.0 and 60°C to 80°C, respectively. Immobilized enzyme showed an increase in pH stability over the studied pH range (3.0–10.0) and stability at temperature up to 80°C. The storage stability and reusability of the immobilized β-glucosidase were improved significantly, with 12.09% activity retention at 30°C after being stored for 25？d and 17.85% residual activity after being repeatedly used for 4 times. The effect of both free and immobilized β-glucosidase enzyme on physicochemical properties of sugarcane juice was also analyzed. 1. Introduction β-Glucosidase (β-D-glucoside glucohydrolase; EC 3.2.1.21) is a part of multienzyme cellulase complex, whose synthesis and action are intricately controlled by regulatory mechanisms in the organisms that produce these enzymes. The enzymatic hydrolysis of cellulose involves three types of cellulase activities (cellobiohydrolases, endoglucanases, and β-glucosidases) working in synergy [1, 2]. β-Glucosidases hydrolyze β-D-glycosidic bond to release nonreducing β-D-glucose residue and terminal aglycone. These are widely used in the various biotechnological processes including aroma and flavour enrichment [3], discoloration of fruit juices prevention [4], and organoleptic properties of citrus fruit juices improvement, in which the bitterness is in part due to a glucosidic compound, naringin (4,5,7-trihydroxyflavanone-7-rhamnoglucoside) [5]. β-Glucosidase also acts as a key enzyme in the enzymatic release of aromatic compounds from glucosidic precursors present in fruits and fermentation products [6]. Transglycosylation reactions by β-glucosidase have great importance in wine or beverage industry because of their abilities to improve the aroma [7]. The synthetic activity of β-glucosidase can be used in the preparation of a variety of compounds such as oligosaccharides and glycoconjugates that have potential for use as agrochemicals and drugs. β-Glucosidase, produced intracellularly by many microorganisms, usually shows a broad specificity and also transferase activity [8]. Nevertheless, the applications of enzyme in
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