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20 ± 0.07 for nucleophile and the proton donor, respectively. Enzyme kinetics study was also performed and the values of (127 ± 6) U mg-1 and (0.78 ± 0.08) mM were obtained for Vmax and Km, respectively. Using the Equilibrium model (EM), the thermal inactivation data were analyzed. ΔHeq, Teq, ΔGinact∗ and ΔGcat∗ were found to be (222 ± 4) kJ mol-1, (323.0 ± 0.1) K, (101.9 ± 0.2) kJ mol-1 and (53.37 ± 0.02) kJ mol-1, respectively. These results show that Rpbgl is less stable with a narrow temperature tolerance compared to other β-glucosidases.This study anal
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