Effective Cleavage of β-1,4-Glycosidic Bond by Functional Micelle with l-Histidine Residue

Abstract

A novel functional surfactant N α-dodecyl-l-histidine (NDH) was synthesized and its micelle was used as mimic of β-1,4-endoglucanase to catalyzed the hydrolysis of methyl-β-d-cellobioside (MCB) under relatively low temperatures (80–110 °C). The results showed that the micelle of NDH displayed excellent catalytic activity for the cleavage of β-1,4-glycosidic bond and the formation of l-histidine-5-d-glucopyranosyl. The micelle-catalyzed first-order reaction rate constant k m of degradation of MCB was calculated. The conversion of MCB and selectivity of reducing sugars (glucose and fructose) could reach 58.9 and 87.1 %, respectively, for a reaction time of 10 h at pH 4.0 and 110 °C. In NDH micelle-catalyzed reaction sugar ester was deduced as the chief product. The reaction pathways of MCB hydrolysis were proposed and the activation energy Ea for the hydrolysis was calculated.