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Improving the specific activity and thermo-stability of alkaline pectate lyase from Bacillus subtilis 168 for bioscouring

elsever. 2017; 
Xiaowen Wang , Zhenghui Lu, Ting Xu, Jonathan Nimal Selvaraj, Li Yi, Guimin Zhang∗
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Mutagenesis Services … About 100 transformants were recovered, forming the site-saturation mutagenesis library. The clones were randomly picked and sequenced, and mutations at the indicated position were confirmed. DNA sequencing was performed by GenScript Co. Ltd. (Nanjing, China) … Get A Quote

摘要

Biocatalysts requires enzymes with high activity and stability under process conditions for efficient application. Several protein improvement strategies were used to improve pectate lyase PEL168 from Bacillus subtilis. Initially, a rationally designed mutant V132F obtained showed 1.7-fold increase in activity with wider pH stability. Meanwhile, highly advantageous mutant K47E selected from a random mutagenesis library displayed 1.8-fold increase in activity, and half-life increased by 2.0-fold at 50 ◦C (T50). The additive effect of these two advantageous mutants K47E/V132F showed 2.2-fold increase in activity than PEL168. To identify beneficial substitution at 47th position, a smarter library was constructed... More

关键词

Pectate lyase Specific activity Rational design Directed evolution Bioscouring