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首页> 外文期刊>Journal of Chemical Technology & Biotechnology >A kinetic model for enzymatic reactions in reverse micellar systems involving water-insoluble substrates and enzyme activators
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A kinetic model for enzymatic reactions in reverse micellar systems involving water-insoluble substrates and enzyme activators

机译:涉及水不溶性底物和酶激活剂的反胶束系统中酶促反应的动力学模型

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摘要

The activity of Chromobacterium viscosum lipase (glycerol-ester hydrolase, EC 3.1.1.3) entrapped in AOT/isooctane reverse micelles was significantly increased by the addition of short chain polyethylene glycols (PEGs) or methoxypolyethylene glycols (MPEGs) for the hydrolysis of olive oil. To understand enzyme activity in the presence of PEG 400 or MPEG 550 molecules, a kinetic model was proposed. The validity of this model was verified by experimental data on the lipase-catalyzed hydrolysis of olive oil in AOT/isooctane reverse micellar systems, in which PEG 400 or MPEG 550 had been added. The large value of the equilibrium constant (k(D)) for enzyme activation indicated that the affinity between C viscosum lipase and PEG 400 or MPEG 550 molecules was very strong. The Michaelis constant (K-m) predicted by the proposed model explained enzymatic reactions more exactly than that by the previously published model. (C) 2003 Society of Chemical Industry.
机译:通过添加短链聚乙二醇(PEG)或甲氧基聚乙二醇(MPEGs)来水解橄榄油,大大提高了包裹在AOT /异辛烷反胶束中的粘杆菌绿脂酶(甘油酯水解酶,EC 3.1.1.3)的活性。 。为了理解在PEG 400或MPEG 550分子存在下的酶活性,提出了动力学模型。该模型的有效性通过在AOT /异辛烷反胶束体系中添加PEG 400或MPEG 550的脂肪酶催化橄榄油水解实验数据验证。酶激活的平衡常数(k(D))很大,表明粘胶脂肪酶与PEG 400或MPEG 550分子之间的亲和力非常强。所提出的模型预测的米氏常数(K-m)比先前发表的模型更准确地解释了酶反应。 (C)2003年化学工业协会。

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