Characterization of EprA, a major extracellular protein of Oenococcus oeni with protease activity

Folio, Patrice; Ritt, Jean-François; Alexandre, Hervé; Remize, Fabienne

doi:10.1016/j.ijfoodmicro.2008.05.039

Cited by 19 publications

(10 citation statements)

References 40 publications

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“…The molecular masses of the putative preproenzymes deduced from the gene sequences are 40.9 kDa (MpAPr1) and 39.1 kDa (CaAPr1). The predicted secretion signal peptide cleavage site for the preproprotein of M. pulcherrima IWBT Y1123 is between Gly 16 and Met 17 , with the first 16 amino acids being the secretion signal peptide. Conflicting results were obtained from different on-line databases and software programs with regard to the prediction of the signal peptide of the enzyme of CaAPr1.…”

Section: Resultsmentioning

confidence: 99%

“…SDS-PAGE analysis was performed on concentrated culture supernatants as previously described (24) with 12.5% bisacrylamide gels on a Bio-Rad Mini-Protean Tetra Cell system (Bio-Rad Labs, Hercules, CA). Zymography was performed at pH 3.5 and with gelatin as a copolymerized substrate (16). To visualize protein bands, gels were stained with Coomassie blue R-250.…”

Section: Methodsmentioning

confidence: 99%

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Identification and Partial Characterization of Extracellular Aspartic Protease Genes from Metschnikowia pulcherrima IWBT Y1123 and Candida apicola IWBT Y1384

Reid

Theron

Toit

et al. 2012

Appl Environ Microbiol

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ABSTRACTThe extracellular acid proteases of non-Saccharomyceswine yeasts may fulfill a number of roles in winemaking, which include increasing the available nitrogen sources for the growth of fermentative microbes, affecting the aroma profile of the wine, and potentially reducing protein haze formation. These proteases, however, remain poorly characterized, especially at genetic level. In this study, two extracellular aspartic protease-encoding genes were identified and sequenced, from two yeast species of enological origin: one gene fromMetschnikowia pulcherrimaIWBT Y1123, namedMpAPr1, and the other gene fromCandida apicolaIWBT Y1384, namedCaAPr1.In silicoanalysis of these two genes revealed a number of features peculiar to aspartic protease genes, and both the MpAPr1 and CaAPr1 putative proteins showed homology to proteases of yeast genera. Heterologous expression ofMpAPr1inSaccharomyces cerevisiaeYHUM272 confirmed that it encodes an aspartic protease. MpAPr1 production, which was shown to be constitutive, and secretion were confirmed in the presence of bovine serum albumin (BSA), casein, and grape juice proteins. TheMpAPr1gene was found to be present in 12 otherM. pulcherrimastrains; however, plate assays revealed that the intensity of protease activity was strain dependent and unrelated to the gene sequence.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Identification and Partial Characterization of Extracellular Aspartic Protease Genes from Metschnikowia pulcherrima IWBT Y1123 and Candida apicola IWBT Y1384

Reid

Theron

Toit

et al. 2012

Appl Environ Microbiol

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“…Growth of Oenococcus oeni depends on the presence of amino acids in the culture medium because of deficiency in corresponding synthetic pathways. This bacterium secretes several proteases which may help to gain access to rare nitrogen sources during malolactic fermentation [77]. nd: not determined.…”

Section: Microbial Proteasesmentioning

confidence: 99%

Enzymes for Wine Fermentation: Current and Perspective Applications

Claus

Mojsov

2018

Fermentation

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Enzymes are used in modern wine technology for various biotransformation reactions from prefermentation through fermentation, post-fermentation and wine aging. Industrial enzymes offer quantitative benefits (increased juice yields), qualitative benefits (improved color extraction and flavor enhancement) and processing advantages (shorter maceration, settling and filtration time). This study gives an overview about key enzymes used in winemaking and the effects of commercial enzyme preparations on process engineering and the quality of the final product. In addition, we highlight on the presence and perspectives of beneficial enzymes in wine-related yeasts and lactic acid bacteria.

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“…Extra-cytoplasmic proteins often have roles in establishing and maintaining interactions between a bacterium and its environment. In O. oeni , secreted proteins have been reported for their proteolytic activity, crucial for survival in the wine environment [33]. One hypothetical protein, OENOO_37002, possesses the domain characteristics of the universal stress protein UspA, suggesting its involvement in stress response.…”

Section: Resultsmentioning

confidence: 99%

A partial proteome reference map of the wine lactic acid bacterium Oenococcus oeni ATCC BAA-1163

et al. 2014

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Oenococcus oeni is the main lactic acid bacterium that carries out the malolactic fermentation in virtually all red wines and in some white and sparkling wines. Oenococcus oeni possesses an array of metabolic activities that can modify the taste and aromatic properties of wine. There is, therefore, industrial interest in the proteins involved in these metabolic pathways and related transport systems of this bacterium. In this work, we report the characterization of the O. oeni ATCC BAA-1163 proteome. Total and membrane protein preparations from O. oeni were standardized and analysed by two-dimensional gel electrophoresis. Using tandem mass spectrometry, we identified 224 different spots corresponding to 152 unique proteins, which have been classified by their putative function and subjected to bioinformatics analysis.

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Characterization of EprA, a major extracellular protein of Oenococcus oeni with protease activity

Cited by 19 publications

References 40 publications

Identification and Partial Characterization of Extracellular Aspartic Protease Genes from Metschnikowia pulcherrima IWBT Y1123 and Candida apicola IWBT Y1384

Identification and Partial Characterization of Extracellular Aspartic Protease Genes from Metschnikowia pulcherrima IWBT Y1123 and Candida apicola IWBT Y1384

Enzymes for Wine Fermentation: Current and Perspective Applications

A partial proteome reference map of the wine lactic acid bacterium Oenococcus oeni ATCC BAA-1163

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