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首页> 外文期刊>Biochemistry >Structure and Functional Investigation of Ligand Binding by a Family 35 Carbohydrate Binding Module (OCBM35) of β-Mannanase of Family 26 Glycoside Hydrolase from Clostridium thermocellum
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Structure and Functional Investigation of Ligand Binding by a Family 35 Carbohydrate Binding Module (OCBM35) of β-Mannanase of Family 26 Glycoside Hydrolase from Clostridium thermocellum

机译:通过热纤维梭菌的26族糖苷水解酶的β-甘露聚糖酶的35族糖结合模块(OCBM35)进行配体结合的结构和功能研究

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摘要

Functional attributes of recombinant QCBM35 (family 35 carbohydrate binding module) of (3-mannanase of family 26 Glycoside Hydrolase from Clostridium thermocellum were deduced by biochemical and in silico approaches. Ligand-binding analysis of expressed CtCBM35 analyzed by affinity-gel electrophoresis and fluorescence spectroscopy exhibited association constants K_a ~ 1.2·10~5 and 3.0·10~5 M~(-1) with locust bean galactomannan and mannotriose, respectively.
机译:通过热化学和计算机模拟的方法推导了热纤梭菌(Clostridium thermocellum)的(26家族糖苷水解酶的3-甘露聚糖酶)的重组QCBM35(35族糖结合模块)的功能特性,通过亲和凝胶电泳和荧光光谱分析了表达的CtCBM35的配体结合分析。与刺槐豆半乳甘露聚糖和甘露三糖的结合常数分别为K_a〜1.2·10〜5和3.0·10〜5 M〜(-1)。

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