Bioinformatic characterization of a triacylglycerol lipase produced by Aspergillus flavus isolated from the decaying seed of Cucumeropsis mannii

Abstract

Lipases are enzymes of industrial importance responsible for the hydrolysis of ester bonds of triglycerides. A lipolytic fungus was isolated and subsequently identified based on the ITS sequence analysis as putative Aspergillus flavus with accession number LC424503. The gene coding for extracellular triacylglycerol lipase was isolated from Aspergillus flavus species, sequenced, and characterised using bioinformatics tools. An open reading frame of 420 amino acid sequence was obtained and designated as Aspergillus flavus lipase (AFL) sequence. Alignment of the amino acid sequence with other lipases revealed the presence GHSLG sequence which is the lipase consensus sequence Gly-X1-Ser-X2-Gly indicating that it a classical lipase. A catalytic active site lid domain composed of TYITDTIIDLS amino acids sequence was also revealed. This lid protects the active site, control the catalytic activity and substrate selectivity in lipases. The 3-Dimensional structural model shared 34.08% sequence identity with a lipase from Yarrowia lipolytica covering 272 amino acid residues of the template model. A search of the lipase engineering database using AFL sequence revealed that it belongs to the class GX-lipase, superfamily abH23 and homologous family abH23.02, molecular weight and isoelectric point values of 46.95 KDa and 5.7, respectively. N-glycosylation sites were predicted at residues 164, 236 and 333, with potentials of 0.7250, 0.7037 and 0.7048, respectively. O-glycosylation sites were predicted at residues 355, 358, 360 and 366. A signal sequence of 37 amino acids was revealed at the N-terminal of the polypeptide. This is a short peptide sequence that marks a protein for transport across the cell membrane and indicates that AFL is an extracellular lipase. The findings on the structural and molecular properties of Aspergillus flavus lipase in this work will be crucial in future studies aiming at engineering the enzyme for biotechnology applications.

Publication DOI: https://doi.org/10.1080/07391102.2022.2035821
Divisions: College of Health & Life Sciences > School of Biosciences
College of Health & Life Sciences > School of Biosciences > Cellular and Molecular Biomedicine
College of Health & Life Sciences
College of Engineering & Physical Sciences > School of Infrastructure and Sustainable Engineering > Chemical Engineering & Applied Chemistry
College of Engineering & Physical Sciences
Additional Information: (c) 2022, The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Funding: The authors wish to acknowledge the Commonwealth scholarship commission in the United Kingdom (scholarship number NGCN-2019-145) for providing the funds for this project.
Uncontrolled Keywords: Extracellular triacylglycerol,amino acid,aspergillus,cucumeropsis,in silico,Structural Biology,Molecular Biology
Publication ISSN: 1538-0254
Full Text Link:
Related URLs: https://www.tan ... 02.2022.2035821 (Publisher URL)
http://www.scop ... tnerID=8YFLogxK (Scopus URL)
PURE Output Type: Article
Published Date: 2022-02-11
Published Online Date: 2022-02-11
Accepted Date: 2022-01-25
Authors: Ezema, Benjamin. O.
Omeje, Kingsley. O.
Bill, Roslyn M. (ORCID Profile 0000-0003-1331-0852)
Goddard, Alan D. (ORCID Profile 0000-0003-4950-7470)
O. Eze, Sabinus Oscar
Fernandez-Castane, Alfred (ORCID Profile 0000-0002-2572-7797)

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