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Overexpression, Purification, and Biochemical Characterization of the Esterase Est0796 from Lactobacillus plantarum WCFS1.
MedLine Citation:
PMID:  23054632     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Lactobacillus plantarum is a lactic acid bacterium that is encountered in an extensive range of foods such as fermented dairy products, meat, vegetables, and bakery products. Given the little molecular information available on the lipolytic activity of L. plantarum, the aim of this study was to clone, purify, and biochemically characterize the esterase coded by gene lp_0796 (Est0796). The esterase was cloned in pET28a and purified in two steps, using solid ammonium sulfate and His tag affinity chromatography. The molecular mass of the purified Est0796 was 28.7 kDa (by SDS-PAGE) and 26.6 kDa (by gel filtration chromatography), pointing to a monomeric structure. Est0796 showed maximum activity at pH 8.0 and 35 °C and toward shorter acyl chain lengths (C(2)-C(4)). The activity was resistant to organic solvents and cations, suggesting that this esterase may play a role in the fermentation of food products.
Authors:
Navarro-González Inmaculada; Sánchez-Ferrer Alvaro; García-Carmona Francisco
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-6
Journal Detail:
Title:  Molecular biotechnology     Volume:  -     ISSN:  1559-0305     ISO Abbreviation:  Mol. Biotechnol.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-11     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9423533     Medline TA:  Mol Biotechnol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Department of Biochemistry and Molecular Biology-A, Faculty of Biology, University of Murcia, Campus Espinardo, 30100, Murcia, Spain, inmaculada.navarro@um.es.
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