摘要
通过超滤、DEAE Sephadex A-50离子交换层析、Sephadex G-100凝胶过滤层析，对一株来自海洋的扩展青霉（Penicillium expansum）所产果胶酶进行分离纯化，得到电泳纯的果胶酶，经SDS-PAGE电泳显示单一条带，且果胶酶亚基的分子质量约为63.96 ku，纯化倍数为24.13，回收率为36.32%。酶学性质研究结果表明，该果胶酶的最适反应温度为50℃，最适pH值5.4，在pH值4.6~6.2比较稳定，Mg2＋、Ca2＋对果胶酶活力有明显激活作用，Cu2＋有明显抑制作用，以果胶粉为底物的Vmax为393.56μg/（min ＆#183; mL），Km为3.34 mg/mL。
Pectinase from marine Penicillium expansum was separated and purified by ultrafiltration, DEAE Sephadex A-50 ion ex-change chromatography, Sephadex G-100 gel filtration chromatography. SDS-PAGE of the purified pectinase revealed a single band at an apparent molecular mass of 63.96 ku. Result showed that pectinase was purified by 24.13 folds with a yield of 36.32%. The en-zymology properties revealed that the optimal reaction temperature was 50℃, and the optimal pH was 5.4. Pectinase was stable in the range of pH4.6-6.2. Mg2＋and Ca2＋had obvious activation on pectinase activity, however Cu2＋had obvious inhibition. Vmax and Km for jelly powder were 393.56μg/（min ＆#183; mL） and 3.34 mg/mL, respectively.
出处
《生物学杂志》
CAS
CSCD
2015年第3期37-41,共5页
Journal of Biology
基金
安徽省教育厅自然科学项目(KJ2012B153)
关键词
海洋扩展青霉
果胶酶
分离纯化
酶学性质
marine Penicillium expansum
pectinase
purification
enzymology properties
