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Review
. 2020 Sep 3;9(9):1231.
doi: 10.3390/foods9091231.

The Role of Yeasts and Lactic Acid Bacteria on the Metabolism of Organic Acids during Winemaking

Ana Mendes Ferreira  1   2   3 , Arlete Mendes-Faia  1   2   3
Affiliations
Review

The Role of Yeasts and Lactic Acid Bacteria on the Metabolism of Organic Acids during Winemaking

Ana Mendes Ferreira et al. Foods. .

Abstract

The main role of acidity and pH is to confer microbial stability to wines. No less relevant, they also preserve the color and sensory properties of wines. Tartaric and malic acids are generally the most prominent acids in wines, while others such as succinic, citric, lactic, and pyruvic can exist in minor concentrations. Multiple reactions occur during winemaking and processing, resulting in changes in the concentration of these acids in wines. Two major groups of microorganisms are involved in such modifications: the wine yeasts, particularly strains of Saccharomyces cerevisiae, which carry out alcoholic fermentation; and lactic acid bacteria, which commonly conduct malolactic fermentation. This review examines various such modifications that occur in the pre-existing acids of grape berries and in others that result from this microbial activity as a means to elucidate the link between microbial diversity and wine composition.

Keywords: fermentation; lactic acid bacteria; organic acids; wine; yeasts.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Schematic representation of the pathway of acids biosynthesis during fermentation. The reactions indicated are catalyzed by the enzymes, encoding by the following genes: PDC1,5,6—pyruvate decarboxylase; ADH—alcohol dehydrogenase; ALD6—aldehyde dehydrogenase; ACS1, ACS2—acetyl-CoA synthetase; FAS1, FAS2—Fatty Acid Synthetase; PYC1,2-cytosol—Pyruvate carboxylase; PDA1, PBD1—subunits of the pyruvate dehydrogenase complex; CIT 1,2,3—Citrate synthase; ACO1,2—Aconitase; IDH1,2—NAD(+)-dependent isocitrate dehydrogenase; KGD1,2, LPD1-α-ketoglutarate dehydrogenase complex; ACH1—Protein for SH-CoA transfer from succinyl-CoA to acetate; LSC1,2—subunits of succinyl-CoA ligase; SDH1,2,3—subunits of succinate dehydrogenase; FRD1—fumarate reductase; FUM1—fumarase; MDH1—mitochondrial malate dehydrogenase; MAE1—mitochondrial malic enzyme.
Figure 2
Figure 2
Schematic representation of the pathway for citrate and malate metabolism by lactic acid bacteria. The reactions indicated are catalyzed by the following enzymes: mleP—malate permease; mleA—malolactic enzyme; citP/maeP—putative citrate permease; citE—citrate lyase; citM—oxaloacetade decarboxylase; ldh—lactate dehydrogenase; pdh—pyruvate dehydrogenase; ackA—acetate kinase; alsS—α-acetolactate synthase; alsD—α-acetolactate decarboxylase; adhE—acetaldehyde dehydrogenase; butA—acetoin dehydrogenase; butB-2,3—butanediol dehydrogenase; TPP—thiamine PPi.
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