Citation:
SONG Shao-Fang, LUAN Yu-Xia, LU Fu-Sui. The Activity of Lipase in Microemulsion-based Gels Catalyzing the Hydrolysis of Glycerol α-Monostearate[J]. Chinese Journal of Applied Chemistry,
;2006, 23(2): 188-192.
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Lipase was immobilized in sodium bis(2-ethylhexyl) sulphosuccinate(AOT)-n-heptane microemulsion as a matrix with gelatin,and its catalytic activity in an organic medium for the hydrolysis of glycerol α-monostearate was studied.Results indicate that the concentrations of gelatin and AOT,the R value(the molar ratio of water to AOT) have effects on the catalytic activity of lipase.The lipase immobilization was optimized when the AOT microemulsion composed of 75% n-heptane,9% buffer and 16% AOT(mass fraction),and the composition of gelatin was 17%,and the R value 72.Kinetic studies showed that when its concentration was constant,lipase in the gel exerted its maximum catalytic activity as the concentration of the substrate reached 0.10 mol/L.The reaction reached its balance after 15 h reaction time.
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