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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| Format: | Article |
| Language: | English |
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Wiley
2016-01-01
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| Series: | Biochemistry Research International |
| Online Access: | http://dx.doi.org/10.1155/2016/4101059 |
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| author | B. Senthilkumar D. Meshachpaul R. Rajasekaran |
| author_facet | B. Senthilkumar D. Meshachpaul R. Rajasekaran |
| author_sort | B. Senthilkumar |
| collection | DOAJ |
| 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 |
| id | doaj-art-0c884deccd0e434da9c1f1ef6ed06431 |
| institution | Kabale University |
| issn | 2090-2247 2090-2255 |
| language | English |
| publishDate | 2016-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Biochemistry Research International |
| spelling | doaj-art-0c884deccd0e434da9c1f1ef6ed064312025-02-03T05:57:08ZengWileyBiochemistry Research International2090-22472090-22552016-01-01201610.1155/2016/41010594101059Geometric Simulation Approach for Grading and Assessing the Thermostability of CALBsB. Senthilkumar0D. Meshachpaul1R. Rajasekaran2Computational Biology Lab, Department of Biotechnology, School of Bio Sciences and Technology, VIT University, Vellore, Tamil Nadu 632014, IndiaComputational Biology Lab, Department of Biotechnology, School of Bio Sciences and Technology, VIT University, Vellore, Tamil Nadu 632014, IndiaComputational Biology Lab, Department of Biotechnology, School of Bio Sciences and Technology, VIT University, Vellore, Tamil Nadu 632014, IndiaCandida 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.http://dx.doi.org/10.1155/2016/4101059 |
| spellingShingle | B. Senthilkumar D. Meshachpaul R. Rajasekaran Geometric Simulation Approach for Grading and Assessing the Thermostability of CALBs Biochemistry Research International |
| title | 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_short | Geometric Simulation Approach for Grading and Assessing the Thermostability of CALBs |
| title_sort | geometric simulation approach for grading and assessing the thermostability of calbs |
| url | http://dx.doi.org/10.1155/2016/4101059 |
| work_keys_str_mv | AT bsenthilkumar geometricsimulationapproachforgradingandassessingthethermostabilityofcalbs AT dmeshachpaul geometricsimulationapproachforgradingandassessingthethermostabilityofcalbs AT rrajasekaran geometricsimulationapproachforgradingandassessingthethermostabilityofcalbs |