화학공학소재연구정보센터
Catalysis Letters, Vol.146, No.7, 1249-1255, 2016
Effective Cleavage of beta-1,4-Glycosidic Bond by Functional Micelle with L-Histidine Residue
A novel functional surfactant N (alpha)-dodecyl-l-histidine (NDH) was synthesized and its micelle was used as mimic of beta-1,4-endoglucanase to catalyzed the hydrolysis of methyl-beta-d-cellobioside (MCB) under relatively low temperatures (80-110 A degrees C). The results showed that the micelle of NDH displayed excellent catalytic activity for the cleavage of beta-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 A degrees 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.