Immobilization of Lipase in Short-channel MesoporousBA-15 Functionalized with Different Groups and Pore Diameters
Date Issued
2008
Date
2008
Author(s)
Huang, Chih-Chuan
Abstract
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 amall amount of Zr(IV) in the synthesis solution. The mesoporous silica with various functional groups including phenol, thio, carboxylic acid, amino, and octyl were alsorepared. They were used as the supports for lipase (from porcine pancreas) immobilization. The large pore facilitated the adsorption of the enzyme. The optimalH 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, andarboxylic 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 groupould 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.
Subjects
lipase
triacetin
functionalized
pore size
Type
thesis
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