Isolation, Purification, and Characterization of the PR Oxidase from Penicillium roqueforti
收藏PubMed Central2026-05-16 收录
下载链接:
https://pmc.ncbi.nlm.nih.gov/articles/PMC90958/
下载链接
链接失效反馈官方服务:
资源简介:
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°C.
PR氧化酶(PR oxidase)是一种可催化PR毒素转化为PR酸的胞外酶,该酶从产紫青霉(Penicillium roqueforti)ATCC 48936的培养液中纯化得到。该酶的等电点(pI)为4.5,分子量约为88 kDa,且为单体蛋白;其最适pH约为4.0,最适反应温度为50℃。
提供机构:
American Society for Microbiology (ASM)



