Title : Intracellular esterase from Lactobacillus casei LILA: nucleotide sequencing, purification, and characterization - Fenster_2003_J.Dairy.Sci_86_1118 |
Author(s) : Fenster KM , Parkin KL , Steels JL |
Ref : J Dairy Sci , 86 :1118 , 2003 |
Abstract :
An esterase gene (estC) was isolated from a genomic library of Lactobacillus casei LILA. The estC gene consisted of a 777 bp open reading frame encoding a putative peptide of 28.9 kDa. A recombinant EstC fusion protein containing a C-terminal six-histidine tag was constructed and purified to electrophoretic homogeneity. Characterization of EstC revealed that it was a serine-dependent dimeric enzyme. Optimum temperature, NaCl concentration, and pH for EstC were determined to be 30 degrees C, 0% NaCl, and pH 5.5, respectively. EstC had significant activity under conditions simulating those of ripening cheese (10 degrees C, 4% NaCl, and pH 5.1). Kinetic constants (KM and Vmax) were determined for EstC action on a variety of ethyl esters and ester compounds consisting of substituted phenyl alcohols and short n-chain fatty acids. For comparison purposes, the previously studied EstA from Lactococcus lactis MG1363 was purified to electrophoretic homogeneity and its substrate selectivity determined in a similar fashion. Different substrate selectivities were observed for EstC and EstA. |
PubMedSearch : Fenster_2003_J.Dairy.Sci_86_1118 |
PubMedID: 12741535 |
Gene_locus related to this paper: lacca-Q8KT44 |
Gene_locus | lacca-Q8KT44 |
Fenster KM, Parkin KL, Steels JL (2003)
Intracellular esterase from Lactobacillus casei LILA: nucleotide sequencing, purification, and characterization
J Dairy Sci
86 :1118
Fenster KM, Parkin KL, Steels JL (2003)
J Dairy Sci
86 :1118