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 · 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 · mL) and 3.34 mg/mL, respectively.
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