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瑞氏木霉β-内切葡聚糖酶的纯化及其部分酶学性质研究
Purification of β-endoglucanase in T. reesei QM9414 and its enzymological study
【摘要】 利用盐析、SephadexG-75和DEAE-SephadexA50层析,从瑞氏木霉Trichoderma reeseiQM9414发酵液中纯化了2个具有β-内切葡聚糖酶活性的组分Eg1和Eg2,分子质量分别为65.47 ku和57.04 ku.其最适温度分别为50℃和55℃,最适pH分别为4.8和5.0,米氏常数Km分别为3.76×10-2g/L和4.20×10-2g/L.根据其酶学性质,这是一类不同于已有的β-内切葡聚糖酶,为瑞氏木霉T.reesei QM9414所产β-内切葡聚糖酶的进一步研究奠定了基础.
【Abstract】 Two active components Eg1 and Eg2 of β-endoglucanase were purified by utilizing salting out,Sephadex G-75 chromatography and DEAE-Sephadex A50 chromatography from the fermentation broth of Trichoderma reesei QM9414.The relative molecular weights of Eg1 and Eg2 were 65.47ku and 57.04ku respectively;The optimal temperatures of Eg1 and Eg2 were 50℃ and 55℃ respectively;the optimal pH was 4.8 and 5.0 and their Michaelis constants were Km=3.76×10-2g/L and Km=4.20×10-2g/L.According to their enzymological characters,they are newly discovered.It seemed that the research built a basis for the further study of β-endoglucanase in T.reesei QM9414.
【Key words】 Trichoderma reesei QM9414; β-endoglucanase; purification; enzymology;
- 【文献出处】 云南大学学报(自然科学版) ,Journal of Yunnan University(Natural Sciences Edition) , 编辑部邮箱 ,2009年03期
- 【分类号】Q78
- 【被引频次】2
- 【下载频次】267