Exploring Cyclodextrin Glycosyltransferase's Thermostability through Molecular Dynamics Simulation

Abstract:

Cyclodextrin glycosyltransferase (EC 2.4.1.19, CGTase) is an important industrial enzyme in the production of cyclodextrins. However, the working conditions are extreme, which often restrict the usage of CGTase. Thermal stability is of great importance for this enzyme. Besides to screen microorganism for CGTase that fit the requirement of biotechnology, it is also hoped that protein engineering can tailor CGTase to meet demands of industry. In this work, molecular dynamics simulations were performed to study thermal stabilization of CGTase C-terminal structured region. Dynamic motions of salt bridges in thermal unstable regions were monitored during the simulations. In the C-terminal region, salt bridge Arg591-Asp640 and Lys652-Glu664 were proposed to be more important for stability than the others. Sheet1 and Sheet3 through the Arg591-Asp640 salt-bridge formation renders the C-terminal stable. The salt bridge Lys652-Glu664 linking sheet4 and sheet5 terminal also contributes to the structural stability of C-terminal. This study is attempt to observe the dynamic behavior of CGTase C-terminal at high temperatures and to understand the factors conferring thermostability of this protein. The results provide specific knowledge about thermal stability in CGTase C-terminal and may help to design biotechnologically improved thermostable proteins.

• Periodical: Advanced Materials Research (Volume 647)
• Pages: 434-437
• DOI: https://doi.org/10.4028/www.scientific.net/AMR.647.434
• Online since: January 2013
• Authors: Yi Fu, Qi Fang Gu
• Keywords: C-Terminal, Cyclodextrin Glycosyltransferase, Molecular Dynamics (MD) Simulation, Salt Bridge, Thermostability

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