Transaminase is a widely studied biocatalyst which plays a significant role in the production of chiral amines. However, the low stability of this enzyme inhibits its application in industry. our current research focusses on exploring various enzyme engineering strategies to improve the thermostability of transaminase. As single mutations point could vastly change the properties of the enzyme, deploying molecular dynamic simulation will give insight on how each mutation point would impact the final enzyme properties. Long-time equilibrium molecular dynamics simulations and steered molecular dynamics simulations are going to be employed to investigate the flexibility and conformation of the enzyme variants. The results of the computational research could provide a molecular insight of the effect of each mutation point as well as the effect of multiple mutation on the protein conformation. These results may also indicate some hot spots and crucial mutation points which could be further studied in the improvement of transaminase stability.