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Oenococcus oeni AWRIB429

ABSTRACT: Analysis of transcriptomic response to SO2 by Oenococcus oeni growing in a continuous culture

PROVIDER: PRJNA713911 | ENA |

REPOSITORIES: ENA

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			Action	DRS
		Other
	SRR15966410.fastq.gz	Fastqsanger.gz
	SRR15966411.fastq.gz	Fastqsanger.gz
	SRR15966412.fastq.gz	Fastqsanger.gz
	SRR15966413.fastq.gz	Fastqsanger.gz

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Oenococcus oeni CGH 11strains vs AWRIB515

Project description:CGH analysis of copy number variation in 11 strains of Oenococcus oeni compared to strain AWRIB515.

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Transcriptomic and proteomic analysis of Oenococcus oeni adaptation to wine stress conditions

Project description:The correct development of malolactic fermentation depends on the capacity of Oenococcus oeni to survive under harsh wine conditions. In this study it was characterized the transcriptomic response of O. oeni PSU-1 during the adaptation to wine-like medium (WLM). The period evaluated was from the inoculation into WLM (12% v/v pH 3.4) until the beginning of malolactic fermentation (8h after inoculation).

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Transcriptomic analysis of Oenococcus oenos response to ethanol shock

Project description:The correct development of malolactic fermentation depends on the capacity of Oenococcus oeni to survive under harsh wine conditions. The presence of ethanol is one of the most stressful factors affecting O. oeni performance. In this study, the effect of ethanol addition (12% vol/vol) on O. oeni PSU-1 has been evaluated using a transcriptomic approach.

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

Project description: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. O. oeni possesses an array of metabolic activities which 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 analyzed by two-dimensional gel electrophoresis. Using tandem mass spectrometry we identified 226 different polypeptides corresponding to 155 unique proteins, which have been classified by their putative function and subjected to bioinformatics analysis.

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