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首页> 外文期刊>Acta Crystallographica Section F >Purification, crystallization and preliminary crystallographic analysis of the catalytic domain of the extracellular cellulase CBHI from Trichoderma harzianum
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Purification, crystallization and preliminary crystallographic analysis of the catalytic domain of the extracellular cellulase CBHI from Trichoderma harzianum

机译:哈茨木霉细胞外纤维素酶CBHI催化结构域的纯化,结晶和初步晶体学分析

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摘要

The filamentous fungus Trichoderma harzianum has a considerable cellulolytic activity that is mediated by a complex of enzymes which are essential for the hydrolysis of microcrystalline cellulose. These enzymes were produced by the induction of T. harzianum with microcrystalline cellulose (Avicel) under submerged fermentation in a bioreactor. The catalytic core domain (CCD) of cellobiohydrolase I (CBHI) was purified from the extracellular extracts and submitted to robotic crystallization. Diffraction-quality CBHI CCD crystals were grown and an X-ray diffraction data set was collected under cryogenic conditions using a synchrotron-radiation source.
机译:丝状真菌哈茨木霉(Trichoderma harzianum)具有相当大的纤维素分解活性,这是由酶的复合物介导的,这些酶对于微晶纤维素的水解至关重要。这些酶是通过在生物反应器中浸没发酵条件下用微晶纤维素(Avicel)诱导哈茨木霉而产生的。从细胞外提取物中纯化纤维二糖水解酶I(CBHI)的催化核心结构域(CCD),并进行自动结晶。生长衍射质量的CBHI CCD晶体,并使用同步辐射源在低温条件下收集X射线衍射数据集。

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