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用于激活牛奶中乳过氧化物酶抗菌系统的固定化双酶体系。

An immobilized two-enzyme system for the activation of the lactoperoxidase antibacterial system in milk.

作者信息

Björck L

出版信息

Biotechnol Bioeng. 1976 Oct;18(10):1463-72. doi: 10.1002/bit.260181013.

Abstract

Lactoperoxidase catalyzes the oxidation of thiocyanate by hydrogen peroxide and an intermediary product is formed with antibacterial properties. The components of this system, with the exception of hydrogen peroxide, are present in milk. H2O2 may be introduced by means of enzymatic generation and thus make the system complete. A two-enzyme system consisting of beta-galactosidase and glucose oxidase has been developed for this purpose. The coupled enzyme reaction is shown to work with high efficiency at the neutral pH of milk although the enzymes as such, particularly lactases suitable for immobilization, have optimal activities at much lower pH values. The results indicate that the lactoperoxidase system may in this way be employed to inactivate bacteria present in milk.

摘要

乳过氧化物酶催化过氧化氢将硫氰酸盐氧化,并形成具有抗菌特性的中间产物。该系统的成分(除过氧化氢外)存在于牛奶中。过氧化氢可通过酶促生成引入,从而使该系统完整。为此已开发出一种由β-半乳糖苷酶和葡萄糖氧化酶组成的双酶系统。尽管这些酶本身,特别是适合固定化的乳糖酶,在低得多的pH值下具有最佳活性,但耦合酶反应在牛奶的中性pH值下显示出高效工作。结果表明,以这种方式乳过氧化物酶系统可用于使牛奶中存在的细菌失活。

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