A novel bacterial carboxylesterase identified in a metagenome derived-clone from Brazilian mangrove sediments.
Mol Biol Rep
; 47(5): 3919-3928, 2020 May.
Article
em En
| MEDLINE
| ID: mdl-32399808
ABSTRACT
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, confirming 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 purified 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.
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Base de dados:
MEDLINE
Assunto principal:
Gammaproteobacteria
/
Carboxilesterase
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article