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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 被引量:1

Purification of β-endoglucanase in T. reesei QM9414 and its enzymological study
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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. 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 65.47 ku and 57.04 ku 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.
出处 《云南大学学报(自然科学版)》 CAS CSCD 北大核心 2009年第3期316-320,共5页 Journal of Yunnan University(Natural Sciences Edition)
基金 西南民族大学自然科学基金项目资助(23444)
关键词 TRICHODERMA REESEI QM9414 β-内切葡聚糖酶 分离纯化 酶学性质 Trichoderma reesei QM9414 β - endoglucanase purification enzymology
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