Clonacion, expresión, caracterización bioquímica parcial y modelado de una esterasa de Acinetobacter Calcoaceticus SP DSM587

  1. Inmaculada Navarro-González 1
  1. 1 Universidad de Murcia, España
Revista:
Biocyt: Biología, Ciencia y Tecnología

ISSN: 2007-2082

Año de publicación: 2013

Volumen: 6

Número: 1

Páginas: 410-425

Tipo: Artículo

DOI: 10.22201/FESI.20072082.2013.6.76113 DIALNET GOOGLE SCHOLAR lock_openAcceso abierto editor

Otras publicaciones en: Biocyt: Biología, Ciencia y Tecnología

Resumen

The aim of this paper has been to clone, express, purify and characterization the EstB from Acinetobacter calcoaceticus encoded by the gen X8895. The esterase was cloned in Pet28a and partially purified. The molecular mass of the purified enzyme was 36 kDa (by SDS) and 68.9 KDa (by gel filtration chromatography). The EstB showed a maximum activity at 35ºC and pH 8 and towards shorter acyl chain lengths (PNPA, PNPB, PNPC) and showed activity about Smethyltiobutanoate, too. The catalytic triad has been predicted by aminoacid sequence alignment and the structure modeling was performed used esterase 1QoR as template.