CAJ | 학술논문

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。
통과초려、DEAE Sephadex A-50리자교환층석、Sephadex G-100응효과려층석，대일주래자해양적확전청매(Penicillium expansum)소산과효매진행분리순화，득도전영순적과효매，경SDS-PAGE전영현시단일조대，차과효매아기적분자질량약위63.96 ku，순화배수위24.13，회수솔위36.32%。매학성질연구결과표명，해과효매적최괄반응온도위50℃，최괄pH치5.4，재pH치4.6~6.2비교은정，Mg2+、Ca2+대과효매활력유명현격활작용，Cu2+유명현억제작용，이과효분위저물적Vmax위393.56μg/(min · mL)，Km위3.34 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.