Banerjee U C
Biochemical Engineering Research and Process Development Centre, Institute of Microbial Technology, Chandigarh, India.
Lett Appl Microbiol. 1993 Jul;17(1):1-3. doi: 10.1111/j.1472-765x.1993.tb01421.x.
Curvularia lunata var. aeria was grown on yeast extract, peptone and carboxymethylcellulose (YPC) medium for the production of extracellular rifamycin oxidase. The enzyme was partially purified through a Sephadex G-75 column. The half lives of rifamycin oxidase at 30 degrees and 40 degrees C were 9 d and 100 min, respectively. The activation and deactivation energies of the partially purified enzyme, calculated from Arrhenius plots, were 5.80 and 35.10 kcal mol-1, respectively. The enzyme exhibited a Km (rifamycin B) value of 0.67 mmol l-1 and a Vmax of 11 mumol h-1.ml. Three metal ions, Fe2+, Ag+ and Hg2+, inhibited the enzyme in the 10-20 mmol l-1 metal ion concentration range. Catalytic activity was not affected by the chelating agent, EDTA.
新月弯孢菌气生变种在酵母提取物、蛋白胨和羧甲基纤维素（YPC）培养基上培养以生产细胞外利福霉素氧化酶。该酶通过Sephadex G - 75柱进行部分纯化。利福霉素氧化酶在30℃和40℃下的半衰期分别为9天和100分钟。根据阿伦尼乌斯图计算，部分纯化酶的活化能和失活能分别为5.80和35.10千卡·摩尔⁻¹。该酶的米氏常数（利福霉素B）值为0.67毫摩尔·升⁻¹，最大反应速度为11微摩尔·小时⁻¹·毫升。在10 - 20毫摩尔·升⁻¹的金属离子浓度范围内，三种金属离子Fe²⁺、Ag⁺和Hg²⁺对该酶有抑制作用。催化活性不受螯合剂乙二胺四乙酸（EDTA）的影响。
