Biochemical diversity of carboxyl esterases and lipases from lake arreo (Spain) : a metagenomic approach
Martínez-Martínez, Mónica (Consejo Superior de Investigaciones Científicas (Espanya). Departamento de Biocatálisis Aplicada)
Alcaide, María (Consejo Superior de Investigaciones Científicas (Espanya). Departamento de Biocatálisis Aplicada)
Tchigvintsev, Anatoli (University of Toronto. Department of Chemical Engineering and Applied Chemistry)
Reva, Oleg (University of Pretoria. Department of Biochemistry)
Polaina, Julio (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Agroquímica y Tecnología de Alimentos (Paterna))
Bargiela, Rafael (Consejo Superior de Investigaciones Científicas (Espanya). Departamento de Biocatálisis Aplicada)
Guazzaroni, María Eugenia (Consejo Superior de Investigaciones Científicas (Espanya). Departamento de Biocatálisis Aplicada)
Chicote, Álvaro (Universidad de Castilla-La Mancha)
Canet, Albert (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química)
Valero Barranco, Francisco (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química)
Rico Eguizabal, Eugenio (Universidad Autónoma de Madrid. Departamento de Ecología)
Guerrero, María del Carmen (Universidad Autónoma de Madrid. Departamento de Ecología)
Yakunin, Alexander F. (University of Toronto. Department of Chemical Engineering and Applied Chemistry)
Ferrer, Manuel (Consejo Superior de Investigaciones Científicas (Espanya). Departamento de Biocatálisis Aplicada)

Fecha:	2013
Resumen:	The esterases and lipases from the α/β hydrolase superfamily exhibit an enormous sequence diversity, fold plasticity, and activities. Here, we present the comprehensive sequence and biochemical analyses of seven distinct esterases and lipases from the metagenome of Lake Arreo, an evaporite karstic lake in Spain (42°46=N' 2°59=W; altitude, 655 m). Together with oligonucleotide usage patterns and BLASTP analysis, our study of esterases/lipases mined from Lake Arreo suggests that its sediment contains moderately halophilic and cold-adapted proteobacteria containing DNA fragments of distantly related plasmids or chromosomal genomic islands of plasmid and phage origins. This metagenome encodes esterases/lipases with broad substrate profiles (tested over a set of 101 structurally diverse esters) and habitat-specific characteristics, as they exhibit maximal activity at alkaline pH (8. 0 to 8. 5) and temperature of 16 to 40°C, and they are stimulated (1. 5 to 2. 2 times) by chloride ions (0. 1 to 1. 2 M), reflecting an adaptation to environmental conditions. Our work provides further insights into the potential significance of the Lake Arreo esterases/lipases for biotechnology processes (i. e. , production of enantiomers and sugar esters), because these enzymes are salt tolerant and are active at low temperatures and against a broad range of substrates. As an example, the ability of a single protein to hydrolyze triacylglycerols, (non)halogenated alkyl and aryl esters, cinnamoyl and carbohydrate esters, lactones, and chiral epoxides to a similar extent was demonstrated.
Ayudas:	Ministerio de Economía y Competitividad CSD2007-00005 European Commission 245226
Derechos:	Aquest material està protegit per drets d'autor i/o drets afins. Podeu utilitzar aquest material en funció del que permet la legislació de drets d'autor i drets afins d'aplicació al vostre cas. Per a d'altres usos heu d'obtenir permís del(s) titular(s) de drets.
Lengua:	Anglès
Documento:	Article ; recerca ; Versió acceptada per publicar
Publicado en:	Applied and Environmental Microbiology, Vol. 79, issue 12 (June 2013) , p. 3553-3562, ISSN 1098-5336

DOI: 10.1128/AEM.00240-13
PMID: 23542620

Postprint 36 p, 3.8 MB

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