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首页> 外文期刊>Applied Microbiology and Biotechnology >Activity of Pseudomonas cepacia lipase in organic media is greatly enhanced after immobilization on a polypropylene support
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Activity of Pseudomonas cepacia lipase in organic media is greatly enhanced after immobilization on a polypropylene support

机译：固定在聚丙烯载体上后，假单胞菌洋葱脂肪酶在有机介质中的活性大大增强

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摘要

The purified lipase from Pseudomonas cepacia was used as free and immobilized enzyme preparation for hydrolysis of p-nitrophenyl palmitate (pNPP) and p-nitrophenyl acetate (pNPA) in organic media. The free enzyme was mixed with bovine serum albumin and lyophilized. Immobilization was on porous polypropylene. Conditions where diffusional limitations of the substrate were not limiting the reaction rate were defined. The specific activity of the lipase was greatly enhanced upon immobilization: 16.5- and 7.8-fold for pNPP and pNPA respectively. Both the free and immobilized lipases followed Michaelis-Menten kinetics in organic solvent despite the heterogeneity (solid/liquid) of the reaction mixture. For pNPP, the activation factor upon immobilization came mainly from a reduction in Km)app while kcat was increased for pNPA.
机译：来自洋葱假单胞菌的纯化脂肪酶用作游离的固定化酶制剂，用于在有机介质中水解对硝基苯甲酸棕榈酸酯（pNPP）和对硝基苯乙酸乙酸酯（pNPA）。将游离酶与牛血清白蛋白混合并冻干。固定在多孔聚丙烯上。定义了底物的扩散限制不限制反应速率的条件。固定后脂肪酶的比活性大大提高：pNPP和pNPA分别为16.5和7.8倍。尽管反应混合物具有异质性（固体/液体），游离和固定化脂肪酶都遵循有机溶剂中的Michaelis-Menten动力学。对于pNPP，固定后的活化因子主要来自km）app的降低，而pNPA的kcat升高。

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