Abstract
Thermotoga maritima derived xylanases are important industrial enzymes owing to extensive thermotolerance and stability under broad pH range This study presents in-silico characterization of Thermotoga maritima derived xylanase A and xylanase B through homology modeling and molecular docking approaches. Analyses of primary and secondary structures revealed net negative charges on both xylanase A and xylanase B. Modular structure of xylanase A exhibited five significant domains including two CBM49, one GlycoHydro10 and two DUF1083. Whereas, structure of xylanase B contained one significant domain i.e. Glyco hydro 10. The amino acid residues Leu-54, Arg-85, Leu-66, Phe-68, Asn-81 and Ile-52 of CBM49 have shown interaction with xylan during docking analyses. Within second CBM49 domain, Tyr-96, Trp-47 and Arg-19 have shown interaction with xylan. No residue of GlycoHydro10 was found to interact with xylan. Whereas, Asn-55, Arg-83, Arg-60 and ILe-118 of DUF1083 interacted with xylan. The Phe-170, Trp-156, Glu-15, Ser-157 and Lys-17 of DUF-1083 domain of xylanase A also showed interaction with xylan. The Glu-15 and Phe-170 of xylanase B showed H-bonding while Lys-565 showed electrostatic interaction with xylan. Comparative phylogenetic analysis of xylanases from Thermotoga genus, showed the complex evolutionary lineage of multimeric xylanase A protein. The findings of this study will lead us towards functional insights of xylanases from Thermotoga maritima and will help the researchers in xylanase enzyme engineering through rational design for developing highly efficient industrial enzymes
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
