Lys-Arg mutation improved the thermostability of Bacillus cereus neutral protease through increased residue interactions
Lys-Arg mutation improved the thermostability of Bacillus cereus neutral protease through increased residue interactions
复制标题
Lys-Arg 突变通过增加残基相互作用提高了蜡样芽胞杆菌中性蛋白酶的热稳定性
DOI：
10.1007/s11274-019-2751-5
复制
发表时间：
2019-11-01
影响因子：
4.1
通讯作者：
Rao, Zhiming
中科院分区：
文献类型：
--
作者：
Osire, Tolbert;Yang, Taowei;Rao, Zhiming
Neutral proteases have broad application as additives in modern laundry detergents and therefore, thermostability is an integral parameter for effective production of protein crystals. To improve thermostability, the contribution of individual residues of Bacillus cereus neutral protease was examined by site-directed mutagenesis. The Lys11Arg and Lys211Arg mutants clearly possessed improved thermostabilities (Tmwere 63 and 61 °C respectively) compared to the wild-type (Tmwas 60 °C). MD simulations further revealed that the mutants had low RMSD and RMSF values compared to wild-type BCN indicating increased stability of the protein structure. Lys11Arg mutant particularly possessed the lowest RMSD values due to increased residue interactions, which resulted in enhanced thermostability. The mutants also displayed strong stability to most inhibitors, organic solvents and surfactants after incubation for 1 h. This study demonstrated Lys-Arg mutation enhanced thermostability of BCN and thus provides insight for engineering stabilizing mutations with improved thermostability for related proteins.
