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Abstract: By using tetraethylorthosilicate as a silica resource and triblock copolymer P123 as a template, the encapsulations of β-galactosidase with three different models of without protection, protection of protective agent and molecular imprinting technique pretreatment were accomplished through modified "fish-in-net" route at pH 5.0. The highest enzymatic activity of β-galactosidase was gained by using pretreatment of molecular imprinting technique. Scanning electron microscopy (SEM) images showed that the matrix of encapsulated β-galactosidase was made of an aggregation of uniform microspheres of 200-300ánm, and N2 adsorption/desorption isotherms demonstrated that the matrix of encapsulated β-galactosidase possessed average Brunauer-Emmett-Teller (BET) pore size of 27á+ and narrow pore size distribution. More importantly, compared with encapsulated β-galactosidase without protection, the hydrolytic activity of encapsulated β-galactosidase pretreated by molecular imprinting technique was about 3 times and 1.8 times, while the enzymatic activity of encapsulated β-galactosidase with the protection of protective agent increased only 1.3-fold when lactose and o-nitrophenyl-β-d-galactopyranoside (ONPG) were used as substrates, respectively. The protective effect of molecular imprinting technique pretreatment on the enzymatic activity after encapsulation was better than that by protective agent
Author keywords: β-Galactosidase, encapsulation, Fish-in-net, molecular imprinting technique, Lactose