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Superactivity of peroxidase solubilized in reversed micellar systems.

作者信息

Setti L, Fevereiro P, Melo E P, Pifferi P G, Cabral J M, Aires-Barros M R

机构信息

Instituto de Tecnologia e Química Biológica, Universidade Nova Lisboa, Oeiras, Portugal.

出版信息

Appl Biochem Biotechnol. 1995 Dec;55(3):207-18. doi: 10.1007/BF02786860.

DOI:10.1007/BF02786860
PMID:8579344
Abstract

Vaccinium mirtyllus peroxidase solubilized in reversed micelles was used for the oxidation of guaiacol. Some relevant parameters for the enzymatic activity, such as pH, w(o) (molar ratio water/surfactant), surfactant type and concentration, and cosurfactant concentration, were investigated. The peroxidase showed higher activities in reversed micelles than in aqueous solution. The stability of the peroxidase in reversed micelles was also studied, namely, the effect of w(o) and temperature on enzyme deactivation. The peroxidase displayed higher stabilities in CTAB/hexanol in isooctane reversed micelles, with half-life times higher than 500 h.

摘要

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本文引用的文献

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The principles of enzyme stabilization. VI. Catalysis by water-soluble enzymes entrapped into reversed micelles of surfactants in organic solvents.酶稳定化原理。VI. 包埋于有机溶剂中表面活性剂反胶束内的水溶性酶的催化作用。
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