Enhancing enzymatic properties by the immobilization method |
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Authors: | S G Cao H Yang L Ma S Q Guo |
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Institution: | (1) The State Key Laboratory of Enzyme Engineering, Jilin University, 130023 Changchun, P.R. China |
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Abstract: | Effects of some immobilized carriers on enzymatic properties have been studied. The following results were obtained: (1) When
cholinesterase was immobilized on the hydrophobic carrier with either α-naphthylamine, benzylamine, orp-methylbenzylamine groups, the affinities of immobilized cholinesterase for toxic organophosphors, GB (Isopnopy 1-methylphophonofluoridate)
and Vx o-ethyl-S-(2-diisopnoylomino-thyl) methyl phosphonothiolate], were enhanced 60–90 times and 700–1200 times, respectively,
whereas the thermal stability of the immobilized cholinesterase increased to 110%. Approximately 82–88% activity of the immobilized
cholinesterase remained after continuously operating for 8 h; and (2) Lipase was immobilized on the carrier that was made
up of 6% polyethylenimine, 1% alginate gel, and 1% glutaraldehyde. The initial reaction rate of the esterification of lauric
acid with lauric alcohol catalyzed by this kind of immobilized lipase was increased 21 times, as compared to lipase powder.
About 72% esterification activity of lipase remained after continuous operating for 10 d. |
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Keywords: | Cholinesterase lipase immobilization |
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