罗克福青霉中PR氧化酶的分离、纯化及特性研究
Isolation, purification, and characterization of the PR oxidase from penicillium roqueforti.
作者信息
Chang SC, Lei WY, Tsai YC, Wei YH
机构信息
Department of Biochemistry, National Yang-Ming University, Taipei, Taiwan, Republic of China.
出版信息
Appl Environ Microbiol. 1998 Dec;64(12):5012-5. doi: 10.1128/AEM.64.12.5012-5015.1998.
Abstract
The PR oxidase, an extracellular enzyme, involved in the conversion of PR toxin into PR acid, was purified from the culture broth of Penicillium roqueforti ATCC 48936. The enzyme has a pI of 4.5 and a molecular mass of approximately 88 kDa, and it is a monomer. The optimum pH for this enzyme is ca. 4.0, and the optimum temperature is 50 degreesC.
摘要
从罗克福特青霉ATCC 48936的培养液中纯化出了参与将PR毒素转化为PR酸的胞外酶PR氧化酶。该酶的等电点为4.5，分子量约为88 kDa，是一种单体。此酶的最适pH约为4.0，最适温度为50℃。
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