ArticleApplied and environmental microbiology2009
Cloning and characterization of an intracellular esterase from the wine-associated lactic acid bacterium Oenococcus oeni.
Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 56 citations in OpenAlex.
- Article
- Lactic acid bacteria isolated from dairy products as potential producers of lipolytic, proteolytic and antibacterial proteins.Applied microbiology and biotechnology · 2019Article
- Synthesis of flavor esters by a novel lipase from3 Biotech · 2019Article
- New Insights Into Cinnamoyl Esterase Activity ofFrontiers in microbiology · 2019Article
- Evidence of the genetic diversity and clonal population structure of Oenococcus oeni strains isolated from different wine-making regions of China.Journal of microbiology (Seoul, Korea) · 2018Article
- Article
- Influence of glycosides on behavior of Oenococcus oeni in wine conditions: growth, substrates and aroma compounds.World journal of microbiology & biotechnology · 2017Article
- A Lactobacillus plantarum esterase active on a broad range of phenolic esters.Applied and environmental microbiology · 2015Article
- Efficient recovery of whole cell proteins in Oenococcus oeni--a comparison of different extraction protocols for high-throughput malolactic starter applications.Folia microbiologica · 2014Article
- A partial proteome reference map of the wine lactic acid bacterium Oenococcus oeni ATCC BAA-1163.Open biology · 2014Article
- A low molecular mass cutinase of Thielavia terrestris efficiently hydrolyzes poly(esters).Journal of industrial microbiology & biotechnology · 2013Article
- Biochemical characterization of a first fungal esterase from Rhizomucor miehei showing high efficiency of ester synthesis.PloS one · 2013Article
- Identification and characterization of a novel cold-adapted esterase from a metagenomic library of mountain soil.Journal of industrial microbiology & biotechnology · 2012Article
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4 authors at 1 institution in 1 country.
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Abstract
We report the cloning and characterization of EstB28, the first esterase to be so characterized from the wine-associated lactic acid bacterium, Oenococcus oeni. The published sequence for O. oeni strain PSU-1 was used to identify putative esterase genes and design PCR primers in order to amplify the corresponding region from strain Ooeni28, an isolate intended for inoculation of wines. In this way a 912-bp open reading frame (ORF) encoding a putative esterase of 34.5 kDa was obtained. The amino acid sequence indicated that EstB28 is a member of family IV of lipolytic enzymes and contains the GDSAG motif common to other lactic acid bacteria. This ORF was cloned into Escherichia coli using an appropriate expression system, and the recombinant esterase was purified. Characterization of EstB28 revealed that the optimum temperature, pH, and ethanol concentration were 40 degrees C, pH 5.0, and 28% (vol/vol), respectively. EstB28 also retained marked activity under conditions relevant to winemaking (10 to 20 degrees C, pH 3.5, 14% [vol/vol] ethanol). Kinetic constants were determined for EstB28 with p-nitrophenyl (pNP)-linked substrates ranging in chain length from C(2) to C(18). EstB28 exhibited greatest specificity for C(2) to C(4) pNP-linked substrates.
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