Biochemical characterization and molecular docking of cloned xylanase gene from Bacillus subtilis RTS expressed in E. coli

doi:10.1016/j.ijbiomac.2020.12.001

	Biochemical characterization and molecular docking of cloned xylanase gene from Bacillus subtilis RTS expressed in E. coli
	Saleem, Aimen 3,4; Waris, Saboora 1,5; Ahmed, Toheed 2; Tabassum, Romana 3,4
刊名	INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
	2021-01-31
卷号	168 页码:310-321
关键词	Cloning Sequencing Genetic characterization AutoDock Vina
ISSN号	0141-8130
DOI	10.1016/j.ijbiomac.2020.12.001
英文摘要	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.
资助项目	Higher Education Commission (HEC), H9 Islamabad, Pakista[PAK-US/HEC/2011/144]
WOS关键词	CELLULASE-FREE XYLANASE ; THERMOSTABLE XYLANASE ; PURIFICATION ; CLONING ; LICHENIFORMIS
WOS研究方向	Biochemistry & Molecular Biology ; Chemistry ; Polymer Science
语种	英语
出版者	ELSEVIER
WOS记录号	WOS:000608018200032
资助机构	Higher Education Commission (HEC), H9 Islamabad, Pakista
内容类型	期刊论文
源URL	[http://ir.ipe.ac.cn/handle/122111/43261]
专题	中国科学院过程工程研究所
通讯作者	Tabassum, Romana
作者单位	1.Quaid i Azam Univ, Dept Biol Sci, Islamabad, Pakistan 2.Chinese Acad Sci, Key Lab Green Proc & Engn, Inst Proc Engn, Beijing 100190, Peoples R China 3.Natl Inst Biotechnol & Genet Engn NIBGE, PO Box577,Jhang Rd 3800, Faisalabad, Pakistan 4.Pakistan Inst Engn & Appl Sci PIEAS, Islamabad, Pakistan 5.Shaheed Zulfiqar Ali Bhutto Med Univ, Dept Mol Biol, Islamabad, Pakistan
推荐引用方式 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.