Simultaneous improvement of the thermostability and activity of lactic dehydrogenase from <i>Lactobacillus rossiae</i> through rational design
Xi Luo, Yifeng Wang, Wei‐Long Zheng, Xiaolong Sun, Gaowei Hu, Longfei Yin, Yingying Zhang, Fengwei Yin, Yongqian Fu
Abstract
LDH to a significant extent. The results of molecular dynamics simulations and molecular structure analysis could explain the mechanisms for the improved performance of the double mutant. This study shows that computer-aided rational design can greatly improve the thermostability of d-lactate dehydrogenase, offering a reference for the modification of other enzymes.
Topics & Concepts
ThermostabilityRational designDirected evolutionChemistryMutantBiochemistryEnzyme kineticsSaturated mutagenesisEnzymeStereochemistryBiologyActive siteGeneticsGeneEnzyme Catalysis and ImmobilizationMicrobial Metabolic Engineering and BioproductionBiofuel production and bioconversion