Microalga Chlorella vulgaris has a wide application as a source of biomass fuel, natural food col oring agent and dietary supplement. Its cell wall consists of multiple layers including cellulose and in order to utilize microalgae, the pre treatment is necessary to breakdown rigid cell walls. β glucosidase (EC 3.2.1.21) is a crucial enzyme to hydrolyze cellulose efficiently. In this study, β glucosidase produced by Trichoderma citrinoviride cultivated on microalgae C. vulgaris was purified to homogeneity with a recovery of 8.5% and spe cific activity of 168.7 U/mg. The purified enzyme was obtained as a single band with the molecular mass of 110 kDa on SDS-PAGE. The optimum pH and temperature for enzyme activity and stability were 4.0 and 50°C, and 8.0 and 30°C, respectively. Metal ions (Mg 2+ , and Zn 2+ ) activated the enzyme activity, whereas SDS inhibited moderately. K m , V max , K cat , and K i values of β glucosidase were 0.96 mM, 300.42 μmol min -1 mg -1 , 2.73 min -1 and 2.83 mM using p nitrophenyl β D glucoside as a substrate, whereas they were 4.30 mM, 24.34 μmol min -1 mg -1 , 0.022 min -1 and 0.53 mM using cellobiose, respectively.
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