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Biochemical characterization and molecular docking of cloned xylanase gene from Bacillus subtilis RTS expressed in E. coli | |
Saleem, Aimen1,2; Waris, Saboora3,4; Ahmed, Toheed5; Tabassum, Romana1,2 | |
2021-01-31 | |
Source Publication | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
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ISSN | 0141-8130 |
Volume | 168Pages:310-321 |
Abstract | This study employed mesophilic Bacillus subtilis RTS strain isolated from soil with high xylanolytic activity. A 642 bp (xyn) xylanase gene (GenBank accession number MT677937) was extracted from Bacillus subtilis RTS and cloned in Escherichia coli BL21 cells using pET21c expression system. The cloned gene belongs to glycoside hydrolase family 11 with protein size of approximately 23 KDa. The recombinant xylanase showed optimal enzymeactivity at 60 degrees C and at pH6.5. Thermostability of recombinant xylanase was observed between the temperature range of 30-60 degrees C. Xylanase also remained stable in different concentration of various organic solvents (ethanol, butanol). This might be due to the formation of protein/organic solvent interface which prevents stripping of essential water molecules from enzyme, thus enzyme conformation and activity remained stable. Finally, the molecular docking analysis through AutoDock Vina showed the involvement of Tyr 108, Arg140 and Pro144 in protein-ligand interaction, which stabilizes this complex. The observed stability of recombinant xylanase at higher temperature and in the presence of organic solvent (ethanol, butanol) suggested possible application of this enzyme in biofuel and other industrial applications. (C) 2020 Elsevier B.V. All rights reserved. |
Keyword | Cloning Sequencing Genetic characterization AutoDock Vina |
DOI | 10.1016/j.ijbiomac.2020.12.001 |
Language | 英语 |
WOS Keyword | CELLULASE-FREE XYLANASE ; THERMOSTABLE XYLANASE ; PURIFICATION ; CLONING ; LICHENIFORMIS |
Funding Project | Higher Education Commission (HEC), H9 Islamabad, Pakista[PAK-US/HEC/2011/144] |
WOS Research Area | Biochemistry & Molecular Biology ; Chemistry ; Polymer Science |
WOS Subject | Biochemistry & Molecular Biology ; Chemistry, Applied ; Polymer Science |
Funding Organization | Higher Education Commission (HEC), H9 Islamabad, Pakista |
WOS ID | WOS:000608018200032 |
Publisher | ELSEVIER |
Citation statistics | |
Document Type | 期刊论文 |
Identifier | http://ir.ipe.ac.cn/handle/122111/43262 |
Collection | 中国科学院过程工程研究所 |
Corresponding Author | Tabassum, Romana |
Affiliation | 1.Natl Inst Biotechnol & Genet Engn NIBGE, PO Box577,Jhang Rd 3800, Faisalabad, Pakistan 2.Pakistan Inst Engn & Appl Sci PIEAS, Islamabad, Pakistan 3.Quaid i Azam Univ, Dept Biol Sci, Islamabad, Pakistan 4.Shaheed Zulfiqar Ali Bhutto Med Univ, Dept Mol Biol, Islamabad, Pakistan 5.Chinese Acad Sci, Key Lab Green Proc & Engn, Inst Proc Engn, Beijing 100190, Peoples R China |
Recommended Citation GB/T 7714 | Saleem, Aimen,Waris, Saboora,Ahmed, Toheed,et al. Biochemical characterization and molecular docking of cloned xylanase gene from Bacillus subtilis RTS expressed in E. coli[J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,2021,168:310-321. |
APA | Saleem, Aimen,Waris, Saboora,Ahmed, Toheed,&Tabassum, Romana.(2021).Biochemical characterization and molecular docking of cloned xylanase gene from Bacillus subtilis RTS expressed in E. coli.INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,168,310-321. |
MLA | Saleem, Aimen,et al."Biochemical characterization and molecular docking of cloned xylanase gene from Bacillus subtilis RTS expressed in E. coli".INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 168(2021):310-321. |
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