Bioprospecting of Thermostable Cellulolytic Enzymes through Modeling and Virtual Screening Method
Cellulolytic enzymes are promising candidates for the use of cellulose in any bioprocess operations and for the disposal of the cellulosic wastes in an environmentally benign manner. Cellulases from thermophiles have the advantage of hydrolyzing cellulose at wider range of operating conditions unlik...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Science Planet Inc.
2017-04-01
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| Series: | Canadian Journal of Biotechnology |
| Online Access: | https://www.canadianjbiotech.com/CAN_J_BIOTECH/Archives/v1/i1/CJB-2017-105.pdf |
| _version_ | 1818639897279332352 |
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| author | R. Navanietha Krishnaraj Dipayan Samanta Anand Kumar Rajesh Sani |
| author_facet | R. Navanietha Krishnaraj Dipayan Samanta Anand Kumar Rajesh Sani |
| author_sort | R. Navanietha Krishnaraj |
| collection | DOAJ |
| description | Cellulolytic enzymes are promising candidates for the use of cellulose in any bioprocess operations and for the disposal of the cellulosic wastes in an environmentally benign manner. Cellulases from thermophiles have the advantage of hydrolyzing cellulose at wider range of operating conditions unlike the normal enzymes. Herein we report the modeled structures of cellulolytic enzymes (endoglucanase, cellobiohydrolase and ß-glucosidase) from a thermophilic bacterium,Clostridium thermocellumand their validation using Root Mean Square Deviation (RMSD) and Ramachandran plot analyses. Further, the molecular interactions of the modeled enzyme with cellulose were analyzed using molecular docking technique. The results of molecular docking showed that the endoglucanase, cellobiohydrolase and ß-glucosidase had the binding affinities of
-10.7, -9.0 and -10.8 kcal/mol, respectively. A correlation between the binding affinity of the endoglucanase with cellulose and the enzyme activity was also demonstrated. The results showed that the binding affinities of cellulases with cellulose could be used as a tool to assess the hydrolytic activity of cellulases. The results obtained could be used in virtual screening of cellulolytic enzymes based on the molecular interactions with the substrate, and aid in developing systems biology models of thermophiles for industrial biotechnology applications. |
| first_indexed | 2024-12-16T23:02:40Z |
| format | Article |
| id | doaj.art-0ba0cbe8b84445f7b28ff3eaf958347a |
| institution | Directory Open Access Journal |
| issn | 2560-8304 |
| language | English |
| last_indexed | 2024-12-16T23:02:40Z |
| publishDate | 2017-04-01 |
| publisher | Science Planet Inc. |
| record_format | Article |
| series | Canadian Journal of Biotechnology |
| spelling | doaj.art-0ba0cbe8b84445f7b28ff3eaf958347a2022-12-21T22:12:39ZengScience Planet Inc.Canadian Journal of Biotechnology2560-83042017-04-0111192510.24870/cjb.2017-000105Bioprospecting of Thermostable Cellulolytic Enzymes through Modeling and Virtual Screening MethodR. Navanietha Krishnaraj0Dipayan Samanta1Anand Kumar2Rajesh Sani3Department of Biotechnology, National Institute of Technology Durgapur, Mahatma Gandhi Avenue, Durgapur 713209, INDIADepartment of Biotechnology, National Institute of Technology Durgapur, Mahatma Gandhi Avenue, Durgapur 713209, INDIADepartment of Biotechnology, National Institute of Technology Durgapur, Mahatma Gandhi Avenue, Durgapur 713209, INDIADepartment of Chemical and Biological Engineering, South Dakota School of Mines and Technology, Rapid City 57701, USACellulolytic enzymes are promising candidates for the use of cellulose in any bioprocess operations and for the disposal of the cellulosic wastes in an environmentally benign manner. Cellulases from thermophiles have the advantage of hydrolyzing cellulose at wider range of operating conditions unlike the normal enzymes. Herein we report the modeled structures of cellulolytic enzymes (endoglucanase, cellobiohydrolase and ß-glucosidase) from a thermophilic bacterium,Clostridium thermocellumand their validation using Root Mean Square Deviation (RMSD) and Ramachandran plot analyses. Further, the molecular interactions of the modeled enzyme with cellulose were analyzed using molecular docking technique. The results of molecular docking showed that the endoglucanase, cellobiohydrolase and ß-glucosidase had the binding affinities of -10.7, -9.0 and -10.8 kcal/mol, respectively. A correlation between the binding affinity of the endoglucanase with cellulose and the enzyme activity was also demonstrated. The results showed that the binding affinities of cellulases with cellulose could be used as a tool to assess the hydrolytic activity of cellulases. The results obtained could be used in virtual screening of cellulolytic enzymes based on the molecular interactions with the substrate, and aid in developing systems biology models of thermophiles for industrial biotechnology applications.https://www.canadianjbiotech.com/CAN_J_BIOTECH/Archives/v1/i1/CJB-2017-105.pdf |
| spellingShingle | R. Navanietha Krishnaraj Dipayan Samanta Anand Kumar Rajesh Sani Bioprospecting of Thermostable Cellulolytic Enzymes through Modeling and Virtual Screening Method Canadian Journal of Biotechnology |
| title | Bioprospecting of Thermostable Cellulolytic Enzymes through Modeling and Virtual Screening Method |
| title_full | Bioprospecting of Thermostable Cellulolytic Enzymes through Modeling and Virtual Screening Method |
| title_fullStr | Bioprospecting of Thermostable Cellulolytic Enzymes through Modeling and Virtual Screening Method |
| title_full_unstemmed | Bioprospecting of Thermostable Cellulolytic Enzymes through Modeling and Virtual Screening Method |
| title_short | Bioprospecting of Thermostable Cellulolytic Enzymes through Modeling and Virtual Screening Method |
| title_sort | bioprospecting of thermostable cellulolytic enzymes through modeling and virtual screening method |
| url | https://www.canadianjbiotech.com/CAN_J_BIOTECH/Archives/v1/i1/CJB-2017-105.pdf |
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