Sequence identification and in silico characterization of novel thermophilic lipases from Geobacillus species

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dc.contributor.authorSurmeli, Yusuf
dc.contributor.authorTekedar, Hasan Cihad
dc.contributor.authorSanli-Mohamed, Gulsah
dc.date.accessioned2024-10-29T17:58:16Z
dc.date.available2024-10-29T17:58:16Z
dc.date.issued2024
dc.departmentTekirdağ Namık Kemal Üniversitesi
dc.description.abstractMicrobial lipases are utilized in various biotechnological areas, including pharmaceuticals, food, biodiesel, and detergents. In this study, we cloned and sequenced Lip21 and Lip33 genes from Geobacillus sp. GS21 and Geobacillus sp. GS33, then we in silico and experimentally analyzed the encoded lipases. For this purpose, Lip21 and Lip33 were cloned, sequenced, and their amino acid sequences were investigated for determination of biophysicochemical characteristics, evolutionary relationships, and sequence similarities. 3D models were built and computationally affirmed by various bioinformatics tools, and enzyme-ligand interactions were investigated by docking analysis using six ligands. Biophysicochemical property of Lip21 and Lip33 was also determined experimentally and the results demonstrated that they had similar isoelectric point (pI) (6.21) and T-m (75.5(degrees)C) values as T-m was revealed by denatured protein analysis of the circular dichroism spectrum and pI was obtained by isoelectric focusing. Phylogeny analysis indicated that Lip21 and Lip33 were the closest to lipases from Geobacillus sp. SBS-4S and Geobacillus thermoleovorans, respectively. Alignment analysis demonstrated that S144-D348-H389 was catalytic triad residues in Lip21 and Lip33, and enzymes possessed a conserved Gly-X-Ser-X-Gly motif containing catalytic serine. 3D structure analysis indicated that Lip21 and Lip33 highly resembled each other and they were alpha/beta hydrolase-fold enzymes with large lid domains. BAN Delta IT analysis results showed that Lip21 and Lip33 had higher thermal stability, compared to other thermostable Geobacillus lipases. Docking results revealed that Lip21- and Lip33-docked complexes possessed common residues (H112, K115, Q162, E163, and S141) that interacted with the substrates, except paranitrophenyl (pNP)-C10 and pNP-C12, indicating that these residues might have a significant action on medium and short-chain fatty acid esters. Thus, Lip21 and Lip33 can be potential candidates for different industrial applications.
dc.identifier.doi10.1002/bab.2529
dc.identifier.endpage175
dc.identifier.issn0885-4513
dc.identifier.issn1470-8744
dc.identifier.issue1en_US
dc.identifier.pmid37908087
dc.identifier.scopus2-s2.0-85175574485
dc.identifier.scopusqualityQ3
dc.identifier.startpage162
dc.identifier.urihttps://doi.org/10.1002/bab.2529
dc.identifier.urihttps://hdl.handle.net/20.500.11776/14172
dc.identifier.volume71
dc.identifier.wosWOS:001096113400001
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherWiley
dc.relation.ispartofBiotechnology and Applied Biochemistry
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectGeobacillus
dc.subjecthomology modeling
dc.subjectmolecular docking
dc.subjectrecombinant lipase
dc.subjectthermostable lipase
dc.titleSequence identification and in silico characterization of novel thermophilic lipases from Geobacillus species
dc.typeArticle

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