木聚糖酶
循环芽孢杆菌
合理设计
蛋白质工程
化学
活动站点
木糖
突变
木二糖
突变体
酶
生物化学
立体化学
材料科学
发酵
纳米技术
基因
作者
Kyoungseon Min,Hoyong Kim,Hyun June Park,Siseon Lee,Ye Jean Jung,Ji Hyun Yoon,Jin-Suk Lee,Kyoungmoon Park,Young Je Yoo,Jeong Chan Joo
标识
DOI:10.1016/j.biortech.2021.125737
摘要
Endo-1,4-β-xylanase is one of the most important enzymes employed in biorefineries for obtaining fermentable sugars from hemicellulosic components. Herein, we aimed to improve the catalytic performance of Bacillus circulans xylanase (Bcx) using a structure-guided rational design. A systematic analysis of flexible motions revealed that the R49 component of Bcx (i) constrains the global conformational changes essential for substrate binding and (ii) is involved in modulating flexible motion. Site-saturated mutagenesis of the R49 residue led to the engineering of the active mutants with the trade-off between flexibility and rigidity. The most active mutant R49N improved the catalytic performance, including its catalytic efficiency (7.51-fold), conformational stability (0.7 °C improvement), and production of xylose oligomers (2.18-fold higher xylobiose and 1.72-fold higher xylotriose). The results discussed herein can be applied to enhance the catalytic performance of industrially important enzymes by controlling flexibility.
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