A novel bacterial carboxylesterase identified in a metagenome derived‑clone from Brazilian mangrove sediments

• Autor(a) principal: Araujo, Francisco J.
• Data de Publicação: 2020
• Outros Autores: Hissa, Denise Cavalcante, Silva, Gabrielly O., Antunes, André Saraiva Leão Marcelo, Nogueira, Vanessa L. R., Gonçalves, Luciana R. B., Melo, Vânia M. M.
• Tipo de documento: Artigo
• Idioma: por
• Título da fonte: Repositório Institucional da Universidade Federal do Ceará (UFC)
• Texto Completo: http://www.repositorio.ufc.br/handle/riufc/62906
• topic: Metagenomic library; 1.4-Butanediol diacrylate esterase; Family VIII; Porticoccus; Heterologous expression

A functional screening of 1152 clones from a plasmid library constructed with DNA extracted from Brazilian mangrove sediments revealed 3 positive clones for ester-hydrolyzing enzymes, or about one lipolytic gene per 1.2 Mb DNA, which corroborates the idea that oil-contaminated mangroves are a good source of novel microbial lipases/esterases. The partial sequence of the clone LipG7 (1179 bp) showed 30.2% of predicted structure identity with a known esterase, confrming LipG7 as a new member of family VIII esterases. LigG7 shared 80% sequence identity with 1,4-butanediol diacrylate esterase from the Gammaprotebacteria Porticoccus hydrocarbonoclasticus, suggesting it belongs to the Porticoccaceae family. LipG7 was heterologously expressed in Escherichia coli Rosetta-Gami DE3; the purifed recombinant enzyme exhibited a predicted molecular weight of 45.2 kDa and exceptional activity towards 4-nitrophenyl butyrate, compared with other recombinant esterases, highlighting its enormous potential for biological applications.