摘要
从氧化葡糖杆菌 SCB32 9菌体中分离纯化得到 L-山梨糖脱氢酶后 ,用 Western印迹法验证了 L-山梨糖脱氢酶只存在于产酸“小菌”。SDS- PAGE电泳测得分子量约为 6 0 0 0 0。动力学性质研究表明它为一个典型的 Michaelis-Menten氏酶 ,对 L -山梨糖作用的 Km 值为 5 2 .7× 10 - 3m ol/ L ,最适作用 p H和温度分别为 7.0和 42°C。Mg2 + 、Ca2 +是酶的激活剂 ,EDTA、Cu2 + 是酶的抑制剂 ,氨基酸组成分析表明酸性氨基酸占 2 4.3% ,碱性氨基酸仅占 7.6 %。
After SDH was isolated and purified from Gluconobacter oxydans SCB329, thin layer chromatography showed that SDH is one of the key enzymes to catalyze the transformation from L sorbose to L sorbosone in the fermentation of vitamin C. Its MW is about 60 000 in the SDS PAGE. Dynamic studies demonstrated that it is a typical Michaelis Menten enzyme with K m of 52.7×10 -3 mol/L for L sorbose. The optimal pH and temperature are 7.0 and 42 °C , respectively. This enzyme can be activated by Mg 2+ and Ca 2+ but inhibited by Cu 2+ and EDTA. It contains 24.3% acidic amino acids and 7.6% alkaline amino acids.
出处
《中国医药工业杂志》
CAS
CSCD
北大核心
2001年第3期102-104,共3页
Chinese Journal of Pharmaceuticals
基金
国家自然科学基金!资助项目 批准号 3 9970 0 2 4
