Immobilization of Lipase in Short-channel MesoporousSBA-15 Functionalized with Different Groups and Pore Diameters

碩士 === 國立臺灣大學 === 化學研究所 === 96 === Short-channel SBA-15 with three different pore diameters (7.0, 8.2, and 9.2 nm) were synthesized by hydrothermal reaction at different temperatures with the aid of a small amount of Zr(IV) in the synthesis solution. The mesoporous silica with various functional gro...

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Bibliographic Details
Main Authors: Chih-Chuan Huang, 黃智詮
Other Authors: Soofin Cheng
Format: Others
Language:zh-TW
Published: 2008
Online Access:http://ndltd.ncl.edu.tw/handle/53819600207984553805
Description
Summary:碩士 === 國立臺灣大學 === 化學研究所 === 96 === Short-channel SBA-15 with three different pore diameters (7.0, 8.2, and 9.2 nm) were synthesized by hydrothermal reaction at different temperatures with the aid of a small amount of Zr(IV) in the synthesis solution. The mesoporous silica with various functional groups including phenol, thio, carboxylic acid, amino, and octyl were also prepared. They were used as the supports for lipase (from porcine pancreas) immobilization. The large pore facilitated the adsorption of the enzyme. The optimal pH value for immobilization of lipase changed with the functional groups, and pH 5 is the best for pure siliceous SBA-15 and those functionalized with phenol, thiol, and carboxylic acid while pH 7.4 is the best for amino functionalized SBA-15. In catalytic hydrolysis of triacetin, highest catalytic activity was achieved at pH 7.4 and in the presence of a small amount of hydrophobic co-solvent. Among the functionalized SBA-15 materials, the one functionalized with amino or octyl groups gave the highest catalytic activity. It is attributed to the amino group could keep in lipase at pH 7.4 through the electrostatic interaction and the octyl group facilitates the approach of triacetin to the active sites of lipase.