Cloning and Characterization of an Intracellular Esterase from the Wine-Associated Lactic Acid Bacterium<i>Oenococcus oeni</i>

Sumby, Krista M.; Matthews, Angela; Grbin, Paul R.; Jiranek, Vladimir

doi:10.1128/aem.01563-09

Cited by 51 publications

(83 citation statements)

References 52 publications

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“…Mammalian HSLs contain a catalytic domain and an associated unique regulatory module in the N-terminal domain [35]. Family IV carboxylesterases have four conserved sequence motifs: the oxyanion region GGGX, the pentapeptide -GDSAG-signature motif, and two C-terminal conserved motifs, -DPLR-and -HGF- [1,38,46]. The deduced amino acid sequence indicates that EstIM1 is similar to other esterases of family IV, as it also contains a GGGX (N-terminal oxyanion region) motif, the pentapeptide GXSXG (a nucleophilic elbow), a DPLR motif (at position 252-255), and an HGF motif (at position 282-284) (Fig.…”

Section: Discussionmentioning

confidence: 99%

Identification and characterization of a novel cold-adapted esterase from a metagenomic library of mountain soil

Rim

Han

et al. 2012

Journal of Industrial Microbiology and Biotechnology

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A novel lipolytic enzyme was isolated from a metagenomic library after demonstration of lipolytic activity on an LB agar plate containing 1% (w/v) tributyrin. A novel esterase gene (estIM1), encoding a lipolytic enzyme (EstIM1), was cloned using a shotgun method from a pFosEstIM1 clone of the metagenomic library, and the enzyme was characterized. The estIM1 gene had an open reading frame (ORF) of 936 base pairs and encoded a protein of 311 amino acids with a molecular mass 34 kDa and a pI value of 4.32. The deduced amino acid sequence was 62% identical to that of an esterase from an uncultured bacterium (ABQ11271). The amino acid sequence indicated that EstIM1 was a member of the family IV of lipolytic enzymes, all of which contain a GDSAG motif shared with similar enzymes of lactic acid microorganisms. EstIM1 was active over a temperature range of 1-50°C, at alkaline pH. The activation energy for hydrolysis of p-nitrophenyl propionate was 1.04 kcal/mol, within a temperature range of 1-40°C. The activity of EstIM1 was about 60% of maximal even at 1°C, suggesting that EstIM1 is efficiently cold-adapted. Further characterization of this cold-adapted enzyme indicated that the esterase may be very valuable in industrial applications.

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Section: Discussionmentioning

confidence: 99%

Identification and characterization of a novel cold-adapted esterase from a metagenomic library of mountain soil

Rim

Han

et al. 2012

Journal of Industrial Microbiology and Biotechnology

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“…Esterases that originate from wine LAB are responsible for both the biosynthesis and hydrolysis of esters (Matthews et al, 2004;Sumby et al, 2009;Brod et al, 2010). Oenococcus oeni, as well as species of Lactobacillus and Pediococcus, is able to hydrolyse esters and Matthews et al (2006) found that significant esterase activity levels remained under wine-like conditions.…”

Section: Malolactic Fermentation Must and Wine Composition Before Inomentioning

confidence: 99%

“…Some of the aroma-related enzymes include β-glucosidase, phenolic acid decarboxylase (PAD), citrate lyase, esterase, protease, peptidases, α-acetolactate synthase and α-acetolactate reductase (Spano et al, 2005;Sumby et al, 2009;Brod et al, 2010;Mtshali et al, 2010), as well as enzymes that play a role in the production of volatile sulphur compounds, including S-adenosylmethionine synthase, cystathionine β/γ-lyase and glutathione reductase (Knoll et al, 2010). Other enzymes of interest that play a negative role in the wholesomeness of the wine, besides those enzymes implicated in biogenic amine production, include those that are involved in ethyl carbamate formation, a potential carcinogen.…”

Section: Introductionmentioning

confidence: 99%

Selection and Characterisation of Oenococcus oeni and Lactobacillus plantarum South African Wine Isolates for Use as Malolactic Fermentation Starter Cultures

Lerm¹,

Engelbrecht²,

Toit³

2016

SAJEV

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This study focused on characterising 23 Oenococcus oeni and 19 Lactobacillus plantarum strains isolated from the South African wine environment for the development of potential commercial malolactic fermentation (MLF) starter cultures. These strains were characterised with regards to oenological important characteristics, including the genetic screening for enzyme-encoding genes (enzymes that are involved/implicated in wine aroma modification, as well as enzymes pertaining to the wholesomeness of the final wine product), their fermentation capabilities, the ability to maintain viability during MLF, as well as the volatile acidity production. A total of three O. oeni and three L. plantarum strains were selected at the completion of this study. These six strains showed the most potential during the characterisation stages of the study and were able to successfully complete MLF in Pinotage wine. It was also found that L. plantarum strains displayed a more diverse enzyme profile than O. oeni strains, particularly with regards to the presence of the aroma-modifying enzymes β-glucosidase and phenolic acid decarboxylase (PAD), which implies the future use of this species in the modification of the wine aroma profile and use as commercial starter culture.

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“…The buffers (100 mM) used were acetic acid-sodium acetate (pH 3 to 5), sodium phosphate (pH 6 to 7), Tris-HCl (pH 8), and glycine-NaOH (pH 9). The optimal temperature was assayed by incubating purified Est_1092 esterase in 50 mM McIlvaine buffer (pH 5.0) at different temperatures (5,20,30,37,40,45,55, and 65°C). For temperature stability measurements, the recombinant esterase was incubated in 50 mM McIlvaine buffer, pH 5.0, at 20, 30, 37, 45, 55, and 65°C for 5, 15, and 30 min and 1, 2, 4, 6, and 20 h. Aliquots were withdrawn at these incubation times to test the remaining activity under standard conditions.…”

Section: Methodsmentioning

confidence: 99%

“…Following induction, the cells were grown at 22°C for 20 h and collected by centrifugation (8,000 ϫ g, 15 min, 4°C). The cells were disrupted, and the Est_1092 protein (GenBank accession number ACT61979.1) was purified by affinity chromatography as described previously (18), except that the bound enzyme was eluted using 150 mM McIlvaine buffer (pH 5.0) (30).…”

Section: Methodsmentioning

confidence: 99%

A Lactobacillus plantarum Esterase Active on a Broad Range of Phenolic Esters

Esteban-Torres

Landete

Reverón

et al. 2015

Appl Environ Microbiol

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bLactobacillus plantarum is the lactic acid bacterial species most frequently found in the fermentation of food products of plant origin on which phenolic compounds are abundant. L. plantarum strains showed great flexibility in their ability to adapt to different environments and growth substrates. Of 28 L. plantarum strains analyzed, only cultures from 7 strains were able to hydrolyze hydroxycinnamic esters, such as methyl ferulate or methyl caffeate. As revealed by PCR, only these seven strains possessed the est_1092 gene. When the est_1092 gene was introduced into L. plantarum WCFS1 or L. lactis MG1363, their cultures acquired the ability to degrade hydroxycinnamic esters. These results support the suggestion that Est_1092 is the enzyme responsible for the degradation of hydroxycinnamic esters on the L. plantarum strains analyzed. The Est_1092 protein was recombinantly produced and biochemically characterized. Surprisingly, Est_1092 was able to hydrolyze not only hydroxycinnamic esters, since all the phenolic esters assayed were hydrolyzed. Quantitative PCR experiments revealed that the expression of est_1092 was induced in the presence of methyl ferulate, an hydroxycinnamic ester, but was inhibited on methyl gallate, an hydroxybenzoic ester. As Est_1092 is an enzyme active on a broad range of phenolic esters, simultaneously possessing feruloyl esterase and tannase activities, its presence on some L. plantarum strains provides them with additional advantages to survive and grow on plant environments. Lactobacillus plantarum is a highly versatile lactic acid bacterial species found in many different ecological niches, such as vegetables, meat, fish, and dairy products, as well as in the gastrointestinal tract (1). The genome of L. plantarum strain WCFS1 was the first to be fully sequenced, and it was, in fact, the first of any of the Lactobacillus genomes to be published (2). When the genome diversity of L. plantarum on a full genome scale was analyzed, it was revealed that L. plantarum strains are predicted to lack 9 to 20% of the genes of the L. plantarum WCFS1 reference genome, and about 50 genes appeared to be specific to strain WCFS1, as they were not found in any other strain (1). This variability confirms the flexibility of L. plantarum in its ability to adapt to different environments and growth substrates.Phenolic compounds are important constituents of food products of plant origin, as they are related to the sensory characteristics of the food and are beneficial to consumer health (3). Therefore, it is interesting to know the metabolic pathways of biosynthesis or degradation of these compounds in bacteria. L. plantarum is the lactic acid bacterium that is the most frequently found in the fermentation of food products of plant origin, being the bacterial model for the study of phenolic compound metabolism (4). Among these compounds, the metabolism of phenolic esters is greatly relevant, as they are widely spread throughout the plant kingdom (3). Esters of phenolic acids mainly belong to two distingui...

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Cloning and Characterization of an Intracellular Esterase from the Wine-Associated Lactic Acid BacteriumOenococcus oeni

Cited by 51 publications

References 52 publications

Identification and characterization of a novel cold-adapted esterase from a metagenomic library of mountain soil

Identification and characterization of a novel cold-adapted esterase from a metagenomic library of mountain soil

Selection and Characterisation of Oenococcus oeni and Lactobacillus plantarum South African Wine Isolates for Use as Malolactic Fermentation Starter Cultures

A Lactobacillus plantarum Esterase Active on a Broad Range of Phenolic Esters

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