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Identification of a novel carbohydrate esterase from Bjerkandera adusta: Structural and function predictions through bioinformatics analysis and molecular modeling

dc.contributor.authorBatista-García, Ramón
dc.contributor.authorValdés, Gilberto
dc.contributor.authorCuervo, Laura
dc.contributor.authorSánchez-Carbente, María
dc.contributor.authorBalcázar, Edgar
dc.contributor.authorLira, Verónica
dc.contributor.authorFolch, Jorge Luis
dc.date.accessioned2025-01-30T07:21:28Z
dc.date.available2025-01-30T07:21:28Z
dc.date.issued2015-01
dc.description.abstractA new gene from Bjerkandera adusta strain UAMH 8258 encoding a carbohydrate esterase (designated as BacesI) was isolated and expressed in Pichia pastoris. The gene had an open reading frame of 1410 bp encoding a polypeptide of 470 amino acid residues, the first 18 serving as a secretion signal peptide. Homology and phylogenetic analyses showed that BaCesI belongs to carbohydrate esterases family 4. Three-dimensional modeling of the protein and normal mode analysis revealed a breathing mode of the active site that could be relevant for esterase activity. Furthermore, the overall negative electrostatic potential of this enzyme suggests that it degrades neutral substrates and will not act on negative substrates such as peptidoglycan or p-nitrophenol derivatives. The enzyme shows a specific activity of 1.118 U mg21 protein on 2-naphthyl acetate. No activity was detected on p-nitrophenol derivatives as proposed from the electrostatic potential data. The deacetylation activity of the recombinant BaCesI was confirmed by measuring the release of acetic acid from several substrates, including oat xylan, shrimp shell chitin, N-acetylglucosamine, and natural substrates such as sugar cane bagasse and grass. This makes the protein very interesting for the biofuels production industry from lignocellulosic materials and for the production of chitosan from chitin.
dc.identifier.other10.1002/prot.24760es_ES
dc.identifier.urihttps://hdl.handle.net/10953/4533
dc.language.isoenges_ES
dc.publisherWileyes_ES
dc.relation.ispartofProteins 2015; 83:533–546es_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES
dc.subjectBjerkandera adustaes_ES
dc.subjectFamily 4 carbohydrate esterase
dc.subjectHeterologous expression
dc.subjectLignocellulosic material degradation
dc.subjectDeacetylase
dc.titleIdentification of a novel carbohydrate esterase from Bjerkandera adusta: Structural and function predictions through bioinformatics analysis and molecular modelinges_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.type.versioninfo:eu-repo/semantics/publishedVersiones_ES

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