The kinetic characteristics of the Aspergillus niger β-glucosidase-catalyzed reaction for the pNPG and G2 substrates, where the v-[S]
0 plot does not show the Michaelis (saturation) curve, was consistently explained not by the transfer reaction but by substrate inhibition. The reactions ere carried out in the presence of acetonitrile CH
3CN (ε≅38) : transglucosylation was not confirmed for the βGA-catalyzed reaction. Moreover, CH
3CN was found to have an effect on (increase in) the kinetic parameters K
S and K
S′, resulting in support of “hydrophobic-driven” ES-complex formation, a proposal presented in a previous study.
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