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Reference type: Journal
Authors: Wu ZF, Dong MX, Lu M, Li ZQ
Article Title: Encapsulation of β-galactosidase from Aspergillus oryzae based on "fish-in-net" approach with molecular imprinting technique.
Publication date: 2010
Journal: Journal of Molecular Catalysis B: Enzymatic
Volume: 63
Issue: (1-2)
Page numbers: 75-80.
DOI: 10.1016/j.molcatb.2009.12.012
Alternative URL: http://www.sciencedirect.com/science/article/B6TGN-4Y0T98B-1/2/d84a359c595e15d02d0f5550aa1b3ce9

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

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