Author(s)

Yueming Li^*, Jianchun Xu, Zhimei Xu

Qingdao Langyatai Group Co., Ltd., Qingdao, China.

Chitosanases EAG1, a classical glycoside hydrolase from Bacillus ehimensis, is relatively unstable with higher temperature. This shortcoming seriously restricts its industrial application. Therefore, it is crucial to clarify the theoretical basis of thermo stability and to produce enzymes with high activity and stability. Using the structural modeling and molecular dynamical simulation, residues Leu84, Gly113, Asp116, Ala207 and Leu286 were believed to be the key residues for structural stability. Then the predicted residue Leu84 was mutated to ALA. It was shown that the L84A mutation can improve the thermal stability of chitosanases EAG1. Together with previous studies, mutations of G113C, D116C, A207C and L286C forms two sulfur bonds can change the thermal stability of EAG1. The results suggest that the thermal stability of EAG1 could be engineered by site-directed mutagenesis on the conserved residues. This protocol could be employed for improving thermal stability of other chitosanases EAG1.

Chitosanases EAG1, Thermal Stability, Structural Modeling, Moleculrar Dynamical Simulation

Li, Y. , Xu, J. and Xu, Z. (2018) A Study of the Structural Properties and Thermal Stability of Chitosanases EAG1 by Molecular Dynamics Simulations. Journal of Biomedical Science and Engineering, 11, 320-326. doi: 10.4236/jbise.2018.1111026.