Template enhanced activity of lipase accommodated in siliceous mesocellular foams.
Lipases were adsorbed in siliceous mesocellular foams containing different amounts of residual template in the nanopores. It is found that the hydrolytic activities of the adsorbed lipases are increased with increasing the contents of template in the mesopores. The triacetin hydrolytic activity of the lipase adsorbed in the foam containing 46% of template can be 13 times higher than that of the lipase adsorbed in the foam without template in the nanopores, and its specific activity is about three times higher than that of the free lipase, showing the hyperactivation effect on lipase resulting from the interaction between the lipase and the surfactant in the nanopores. The immobilized lipase cross-linked with glutaraldehyde can retain up to 88% of its original activity after six hydrolysis reaction test. This work provides a new strategy to enhance the activity of immobilized lipase in mesoporous materials.
State Key Laboratory of Catalysis, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, P.O. Box 110, Dalian 116023, China.
Yanmei
Y
Zhang
Lifang
L
Zhao
Jun
J
Li
Huidong
H
Zhang
Liangyu
L
Zheng
Shugui
S
Cao
Can
C
Li
D001426:Bacterial Proteins / Q000737:chemistry*; D016956:Burkholderia cepacia / Q000201:enzymology*; D002384:Catalysis; D004800:Enzymes, Immobilized / Q000737:chemistry*; D006868:Hydrolysis; D008049:Lipase / Q000737:chemistry*; D049329:Nanostructures / Q000737:chemistry*; D036103:Nanotechnology / Q000379:methods*; D016062:Porosity
D001426:Bacterial Proteins; D004800:Enzymes, Immobilized; D008049:Lipase