Geometric Simulation Approach for Grading and Assessing the Thermostability of CALBsReport as inadecuate

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Biochemistry Research International - Volume 2016 2016, Article ID 4101059, 7 pages -

Research ArticleComputational Biology Lab, Department of Biotechnology, School of Bio Sciences and Technology, VIT University, Vellore, Tamil Nadu 632014, India

Received 30 November 2015; Accepted 16 March 2016

Academic Editor: Tzi Bun Ng

Copyright © 2016 B.
Senthilkumar et al.
This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Candida antarctica lipase B CALB is a known stable and highly active enzyme used widely in biodiesel synthesis.
In this work, the stability of native 4K6G and mutant 4K5Q CALB was studied through various structural parameters using conformational sampling approach.
The contours of polar surface area and surface area of mutant CALB were 11357.67 Å

and 30007.4 Å

, respectively, showing an enhanced stability compared to native CALB with a statistically significant value of < 0.0001.
Moreover, simulated thermal denaturation of CALB, a process involving dilution of hydrogen bond, significantly shielded against different intervals of energy application in mutant CALB revealing its augmentation of structural rigidity against native CALB.
Finally, computational docking analysis showed an increase in the binding affinity of CALB and its substrate triglyceride in mutant CALB with Atomic Contact Energy ACE of −91.23 kcal-mol compared to native CALB ACE of −70.3 kcal-mol.
The computational observations proposed that the use of mutant CALB 4K5Q could serve as a best template for production of biodiesel in the future.
Additionally, it can also be used as a template to identify efficient thermostable lipases through further mutations.

Author: B.
Senthilkumar, D.
Meshachpaul, and R.



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