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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Expression, crystal structure and cellulase activity of the thermostable cellobiohydrolase Cel7A from the fungus Humicola grisea var. thermoidea
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Expression, crystal structure and cellulase activity of the thermostable cellobiohydrolase Cel7A from the fungus Humicola grisea var. thermoidea

机译：表情,晶体结构和纤维素酶活动的耐热性的cellobiohydrolase从真菌Cel7A Humicola菌var。

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摘要

Glycoside hydrolase family 7 (GH7) cellobiohydrolases (CBHs) play a key role in biomass recycling in nature. They are typically the most abundant enzymes expressed by potent cellulolytic fungi, and are also responsible for the majority of hydrolytic potential in enzyme cocktails for industrial processing of plant biomass. The thermostability of the enzyme is an important parameter for industrial utilization. In this study, Cel7 enzymes from different fungi were expressed in a fungal host and assayed for thermostability, including Hypocrea jecorina Cel7A as a reference. The most stable of the homologues, Humicola grisea var. thermoidea Cel7A, exhibits a 10 degrees C higher melting temperature (T-m of 72.5 degrees C) and showed a 4-5 times higher initial hydrolysis rate than H. jecorina Cel7A on phosphoric acid-swollen cellulose and showed the best performance of the tested enzymes on pretreated corn stover at elevated temperature (65 degrees C, 24 h). The enzyme shares 57% sequence identity with H. jecorina Cel7A and consists of a GH7 catalytic module connected by a linker to a C-terminal CBM1 carbohydrate-binding module. The crystal structure of the H. grisea var. thermoidea Cel7A catalytic module (1.8 angstrom resolution; R-work and R-free of 0.16 and 0.21, respectively) is similar to those of other GH7 CBHs. The deviations of several loops along the cellulose-binding path between the two molecules in the asymmetric unit indicate higher flexibility than in the less thermostable H. jecorina Cel7A.
机译：糖苷水解酶家族7 (GH7)cellobiohydrolases (CBHs)中发挥重要的作用生物质循环。最丰富的酶表达的强大纤维素分解真菌,还负责大多数的水解酶的潜能鸡尾酒工业加工的植物生物质。工业利用率的重要参数。在这项研究中,从不同的真菌Cel7酶在真菌表示主机和化验耐热性,包括Hypocrea jecorinaCel7A作为参考。homologues, Humicola grisea刺thermoideaCel7A,展品高出10摄氏度融化温度(t m 72.5摄氏度)和显示最初的水解速度比H高4 - 5倍。在磷酸acid-swollen jecorina Cel7A纤维素和显示的最佳性能酶在玉米秸秆预处理进行了测试高温(65度,24 h)。酶57%股票序列身份与H。jecorina Cel7A和由GH7催化c端CBM1模块由链接器连接carbohydrate-binding模块。结构的h .菌var. thermoidea Cel7A催化模块(1.8埃分辨率;,有空分别为0.16和0.21)类似于其他GH7 CBHs。偏差的几个循环的cellulose-binding两个分子之间的路径在不对称单位显示更高灵活性比少耐热性的H。

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