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首页> 外文期刊>Advances in Enzyme Research >Isolation, purification and characterization of carboxymethyl cellulase (CMCase) from endophytic Fusarium oxysporum producing podophyllotoxin
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Isolation, purification and characterization of carboxymethyl cellulase (CMCase) from endophytic Fusarium oxysporum producing podophyllotoxin

机译：内生镰刀菌产鬼臼毒素羧甲基纤维素酶（CMCase）的分离，纯化和鉴定

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摘要

Endophytic fungus Fusarium oxysporum is a rich source of cellulases. In the present study, the highest activity was reported at 28 ° C, pH 5.6 with 2% Carboxymethyl cellulose (CMC) as carbon source. CMC was purified using Sephadex G and DEAE cellulose chromatography to 15.9 folds and the molecular weight was determined to be 84 kDa by SDS-PAGE analysis and was subsequently characterized. The purified enzyme was stable over the pH range from 4.0 to 8.0 and at temperatures below 50 ° C. The enzyme was highly active on CMC and reduced or no activity on Avicel, cellobiose and it was suggested to be CMCase/endoglucanase. The activity of endoglucanase was enhanced in the presence of MgCl2, CoCl2, FeCl3, CaCl2, FeCl2 and intensive to HgCl2. The purified enzyme showed its optimum activity at pH 5.0 - 6.0 and was quite stable at 50 ° C for 30 min and retained 45% of original activity.
机译：内生真菌尖孢镰刀菌是纤维素酶的丰富来源。在本研究中，据报道最高活性是在28°C，pH 5.6和2％羧甲基纤维素（CMC）作为碳源的情况下进行的。使用Sephadex G和DEAE纤维素色谱将CMC纯化至15.9倍，并通过SDS-PAGE分析确定分子量为84 kDa，然后进行表征。纯化的酶在4.0至8.0的pH范围内和低于50°C的温度下均稳定。该酶对CMC具有高活性，对Avicel，纤维二糖的活性降低或没有活性，建议为CMCase /内切葡聚糖酶。内切葡聚糖酶的活性在MgCl2，CoCl2，FeCl3，CaCl2，FeCl2的存在下得到增强，并向HgCl2集中。纯化的酶在pH 5.0-6.0下显示出最佳活性，并在50°C下稳定30分钟，并保留原始活性的45％。

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