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首页> 外文期刊>Protein Expression and Purification >Purification and characterization of recombinant endoglucanase of Trichoderma reesei expressed in Saccharomyces cerevisiae with higher glycosylation and stability
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Purification and characterization of recombinant endoglucanase of Trichoderma reesei expressed in Saccharomyces cerevisiae with higher glycosylation and stability

机译：在酿酒酵母中表达的具有较高糖基化和稳定性的里氏木霉重组内切葡聚糖酶的纯化和鉴定

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摘要

Cel5A (endoglucanase 11) of Trichoderma reesei was expressed in Saccharomyces cerevisiae then purified. Two components (Cl and C2) of recombinant Cel5A with different glycosylation were obtained. Purified Cl had a larger molecular mass (57 kDa) than that of the native Cel5A produced by T. reesei (48 kDa) due to the different extents of asparagines-linked glycosylation. There was no significant difference in enzymatic activity between the Cl and the native Cel5A from T reesei. Cl treated with Endoglycosidase H had a molecular mass of 54 kDa and retained about 88% of its original activity. Unpurified C2 was larger form of hyperglycosylation proteins. Its molecular mass was larger than 85 kDa till up to 200 kDa. It still retained activity regardless of its magnitude molecular mass. With increased glycosylation extent of the enzyme components (C2 > Cl > native Cel5A), the pH range of activity become wider, and thermal stability become higher. (c) 2007 Elsevier Inc. All rights reserved.
机译：里氏木霉的Cel5A（内切葡聚糖酶11）在酿酒酵母中表达，然后纯化。获得具有不同糖基化的重组Cel5A的两个组分（C1和C2）。由于天冬酰胺连接的糖基化程度不同，纯化的Cl具有比里氏木霉产生的天然Cel5A（48 kDa）更大的分子量（57 kDa）。 Cl和来自里氏木霉的天然Cel5A之间的酶活性没有显着差异。用糖苷内切酶H处理的C1的分子量为54kDa，并保留其原始活性的约88％。未纯化的C2是较大形式的高糖基化蛋白。其分子量大于85 kDa，直至200 kDa。无论其分子量大小如何，它仍然保持活性。随着酶成分的糖基化程度增加（C2> Cl>天然Cel5A），活性的pH范围变宽，热稳定性变高。 （c）2007 Elsevier Inc.保留所有权利。

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