Clonacion, expresión, caracterización bioquímica parcial y modelado de una esterasa de Acinetobacter Calcoaceticus SP DSM587
- 1 Universidad de Murcia, España
ISSN: 2007-2082
Year of publication: 2013
Volume: 6
Issue: 1
Pages: 410-425
Type: Article
More publications in: Biocyt: Biología, Ciencia y Tecnología
Abstract
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.