Geometric Simulation Approach for Grading and Assessing the Thermostability of CALBs
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 surfac...
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fthindawi:oai:hindawi.com:10.1155/2016/4101059 2023-05-15T13:59:59+02:00 Geometric Simulation Approach for Grading and Assessing the Thermostability of CALBs B. Senthilkumar D. Meshachpaul R. Rajasekaran 2016 https://doi.org/10.1155/2016/4101059 en eng Biochemistry Research International https://doi.org/10.1155/2016/4101059 Copyright © 2016 B. Senthilkumar et al. Research Article 2016 fthindawi https://doi.org/10.1155/2016/4101059 2019-05-26T05:49:10Z 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 Å2 and 30007.4 Å2, respectively, showing an enhanced stability compared to native CALB with a statistically significant P 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. Article in Journal/Newspaper Antarc* Antarctica Hindawi Publishing Corporation Biochemistry Research International 2016 1 7 |
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Hindawi Publishing Corporation |
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English |
description |
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 Å2 and 30007.4 Å2, respectively, showing an enhanced stability compared to native CALB with a statistically significant P 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. |
format |
Article in Journal/Newspaper |
author |
B. Senthilkumar D. Meshachpaul R. Rajasekaran |
spellingShingle |
B. Senthilkumar D. Meshachpaul R. Rajasekaran Geometric Simulation Approach for Grading and Assessing the Thermostability of CALBs |
author_facet |
B. Senthilkumar D. Meshachpaul R. Rajasekaran |
author_sort |
B. Senthilkumar |
title |
Geometric Simulation Approach for Grading and Assessing the Thermostability of CALBs |
title_short |
Geometric Simulation Approach for Grading and Assessing the Thermostability of CALBs |
title_full |
Geometric Simulation Approach for Grading and Assessing the Thermostability of CALBs |
title_fullStr |
Geometric Simulation Approach for Grading and Assessing the Thermostability of CALBs |
title_full_unstemmed |
Geometric Simulation Approach for Grading and Assessing the Thermostability of CALBs |
title_sort |
geometric simulation approach for grading and assessing the thermostability of calbs |
publisher |
Biochemistry Research International |
publishDate |
2016 |
url |
https://doi.org/10.1155/2016/4101059 |
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Antarc* Antarctica |
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Antarc* Antarctica |
op_relation |
https://doi.org/10.1155/2016/4101059 |
op_rights |
Copyright © 2016 B. Senthilkumar et al. |
op_doi |
https://doi.org/10.1155/2016/4101059 |
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Biochemistry Research International |
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2016 |
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1 |
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7 |
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1766268912014458880 |