MIPdatabase
Authors: Gong W, Song XJ, Wang J
Article Title: Study on lipase conformation recording and its stability.
Publication date: 2006
Journal: Journal of Zhejiang University (Engineering Science)
Volume: 40
Issue: (5)
Page numbers: 841-844.
Alternative URL: http://en.cnki.com.cn/Article_en/CJFDTotal-ZDZC200605022.htm
Abstract: The preparation process and catalytic characteristic of a novel immobilized enzyme-'recorded enzyme' were investigated. Lipase and lauric acid were added into a copolymer system, which contained four different kinds of PEG200(400)-di(meth)acrylate ester and trimethylolpropane trimethacrylate. Polymerization was initiated by ultraviolet irradiation and lauric acid was extracted by organic solvent. Then four recorded lipase polymers of immobilizing lipase conformation were obtained. The results showed that the activity of recorded lipase with PEG400-diacrylate as the function monomer is twice that of soluble lipase and that the stability is enhanced greatly. Recorded lipases retain more than 75%, 50% and 70% of their initial activity under conditions of strong acid, strong alkali and high temperature, respectively. After immersing recorded lipases into precipitation denaturants for 30 days, recorded lipases retain at least 50% of their initial activity
Template and target information: bioimprinting
Author keywords: conformation, lipase, molecular imprinting, stability
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