title: Effect of surface hydrophobicity/hydrophilicity of mesoporous supports on the activity of immobilized lipase.
abstract: Taking advantage of the virtue of hydrophilic surface, lipase was firstly immobilized on SBA-15 as a support. Then the surface of the SBA-15 with enzyme entrapped inside the channels was modified by grafting with organic moieties. It has been found that the silylation with n-decyltrimethoxysilane (DE) and 3-(trimethoxysilyl)propyl methacrylate (MA) following the lipase immobilization increases the surface hydrophobicity. But the surface modified by MA shows more hydrophilicity than that modified by DE. The activity assay indicates that the hydrolytic activity for the hydrolysis of insoluble or partly soluble substrates increases with enhanced surface hydrophobicity.
authors.affiliation: The Key Laboratory of Science and Technology of Controllable Chemical Reactions, Beijing University of Chemical Technology, Beijing 100029, PR China.
authors.forename: Jing
authors.initials: J
authors.lastname: He
authors.forename: Yan
authors.initials: Y
authors.lastname: Xu
authors.forename: Hui
authors.initials: H
authors.lastname: Ma
authors.forename: Qiong
authors.initials: Q
authors.lastname: Zhang
authors.forename: David G
authors.initials: DG
authors.lastname: Evans
authors.forename: Xue
authors.initials: X
authors.lastname: Duan
mesh_terms: D000818:Animals; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism; D010179:Pancreas / Q000201:enzymology; D012822:Silicon Dioxide / Q000737:chemistry* / Q000378:metabolism; D013552:Swine
chemical_list: D004800:Enzymes, Immobilized; C509969:SBA-15; D012822:Silicon Dioxide; D008049:Lipase