黑曲霉产纤维素酶系中内切酶的纯化和性质

Purification and properties of an endo-β-glucanase from a commercial preparation of Aspergillus niger

目的从黑曲霉产纤维素酶系中分离纯化一种内切酶,并对其性质进行研究。方法硫酸铵盐析、Sephadex G100脱盐、DEAE FF弱阴离子交换柱层析,再经SDS-PAGE电泳标定其纯度及分子量。结果从黑曲霉发酵粉中分离纯化出了一种电泳纯的内切β-葡聚糖苷酶,SDS-PAGE分析该内切酶的分子量为26.4kD。结论实验采用的分离纯化方案稳定可行,酶学性质表明,该酶的最适反应温度是55℃,最适pH为4.8。

OBJECTIVE In this contribution, an endo-β-glucanase was isolated and purified from a commercial preparation of Aspergillus niger. Its properties was studied. METHODS The endo-β-glucanase was isolated and purified by means of the ammonium sulfate precipitation, Sephadex G100 and DEAE FF. The molecular mass of the endo-β-glucanase was estimated by SDSPAGE.. RESULTS The experiment showed that an endo-β-glucanase with electrophoretic grade was isolated and purified,and the molecular mass was 26.4kD as estimated by SDS-PAGE. CONCLUSION The experiment indicated that the program of the purification was feasible. The optimal reaction temperature of the endoglucanase was 55℃ ,and the optimal pH was 4.8.