scholarly journals Malolactic enzyme from Oenococcus oeni

Bioengineered ◽  
2013 ◽  
Vol 4 (3) ◽  
pp. 147-152 ◽  
Author(s):  
Christina Schümann ◽  
Herbert Michlmayr ◽  
Andrés M. del Hierro ◽  
Klaus D. Kulbe ◽  
Vladimir Jiranek ◽  
...  
Keyword(s):  
Oenococcus Oeni ◽  
Malolactic Enzyme

Surface Display of Malolactic Enzyme from Oenococcus oeni on Saccharomyces cerevisiae

2013 ◽  
Vol 169 (8) ◽  
pp. 2350-2361 ◽  
Author(s):  
Xiuyan Zhang ◽  
Xiaoyan Hou ◽  
Fang Liang ◽  
Fusheng Chen ◽  
Xiaohong Wang
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Surface Display ◽  
Oenococcus Oeni ◽  
Malolactic Enzyme

scholarly journals l-Malate (−2) Protonation State is Required for Efficient Decarboxylation to l-Lactate by the Malolactic Enzyme of Oenococcus oeni

Molecules ◽  
2020 ◽  
Vol 25 (15) ◽  
pp. 3431
Author(s):  
Waldo Acevedo ◽  
Pablo Cañón ◽  
Felipe Gómez-Alvear ◽  
Jaime Huerta ◽  
Daniel Aguayo ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Malic Acid ◽  
Sequence Similarity ◽  
Isothermal Calorimetry ◽  
Homology Model ◽  
Binding Pocket ◽  
Oenococcus Oeni ◽  
Ligand Docking ◽  
Malolactic Enzyme ◽  
Dynamics Simulations

Malolactic fermentation (MLF) is responsible for the decarboxylation of l-malic into lactic acid in most red wines and some white wines. It reduces the acidity of wine, improves flavor complexity and microbiological stability. Despite its industrial interest, the MLF mechanism is not fully understood. The objective of this study was to provide new insights into the role of pH on the binding of malic acid to the malolactic enzyme (MLE) of Oenococcus oeni. To this end, sequence similarity networks and phylogenetic analysis were used to generate an MLE homology model, which was further refined by molecular dynamics simulations. The resulting model, together with quantum polarized ligand docking (QPLD), was used to describe the MLE binding pocket and pose of l-malic acid (MAL) and its l-malate (−1) and (−2) protonation states (MAL− and MAL2−, respectively). MAL2− has the lowest ∆Gbinding, followed by MAL− and MAL, with values of −23.8, −19.6, and −14.6 kJ/mol, respectively, consistent with those obtained by isothermal calorimetry thermodynamic (ITC) assays. Furthermore, molecular dynamics and MM/GBSA results suggest that only MAL2− displays an extended open conformation at the binding pocket, satisfying the geometrical requirements for Mn2+ coordination, a critical component of MLE activity. These results are consistent with the intracellular pH conditions of O. oeni cells—ranging from pH 5.8 to 6.1—where the enzymatic decarboxylation of malate occurs.

scholarly journals Absence of Malolactic Activity Is a Characteristic of H+-ATPase-Deficient Mutants of the Lactic Acid Bacterium Oenococcus oeni

2003 ◽  
Vol 69 (4) ◽  
pp. 1973-1979 ◽  
Author(s):  
Delphine Galland ◽  
Raphaëlle Tourdot-Maréchal ◽  
Maud Abraham ◽  
Ky Son Chu ◽  
Jean Guzzo
Keyword(s):  
Lactic Acid ◽  
Regulatory Protein ◽  
Oenococcus Oeni ◽  
Growth Conditions ◽  
Pcr Analysis ◽  
Rt Pcr ◽  
Regulation Of Expression ◽  
Gene Encoding ◽  
Malolactic Enzyme ◽  
Malate Metabolism

ABSTRACT The lack of malolactic activity in H+-ATPase-deficient mutants of Oenococcus oeni selected previously was analyzed at the molecular level. Western blot experiments revealed a spot at 60 kDa corresponding to the malolactic enzyme only in the parental strain. Moreover, the mleA transcript encoding the malolactic enzyme was not detected by reverse transcription (RT)-PCR analysis of mutants. These results suggest that the malolactic operon was not transcribed in ATPase-deficient mutants. The mleR gene encoding a LysR-type regulatory protein which should be involved in expression of the malolactic genes was described previously for O. oeni. Results obtained in this study show that the mleR transcript was not detected in the mutants by RT-PCR. No mutation in the nucleotide sequences of the mleR gene and the malolactic operon was found. The effect of a reduction in H+-ATPase activity on l-malate metabolism was then investigated by using other malolactic bacteria. Spontaneous H+-ATPase-deficient mutant strains of Lactococcus lactis and Leuconostoc mesenteroides were isolated by using neomycin resistance. Two mutants were selected. These mutants exhibited ATPase activities that were reduced to 54 and 70% of the activities obtained for the L. lactis and L. mesenteroides parental strains, respectively. These mutants were also acid sensitive. However, in contrast to the ATPase-deficient mutants of O. oeni, activation of l-malate metabolism was observed with the L. lactis and L. mesenteroides mutants under optimal or acidic growth conditions. These data support the suggestion that expression of the genes encoding malolactic enzymes in O. oeni is regulated by the mleR product, as it is in L. lactis. Nevertheless, our results strongly suggest that there is a difference between the regulation of expression of the malolactic locus in O. oeni and the regulation of expression of this locus in less acidophilic lactic acid bacteria.

scholarly journals Heterologous expression of Oenococcus oeni malolactic enzyme in Lactobacillus plantarum for improved malolactic fermentation

AMB Express ◽  
2012 ◽  
Vol 2 (1) ◽  
pp. 19 ◽  
Author(s):  
Christina Schümann ◽  
Herbert Michlmayr ◽  
Reinhard Eder ◽  
Andrés M del Hierro ◽  
Klaus D Kulbe ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Lactobacillus Plantarum ◽  
Malolactic Fermentation ◽  
Oenococcus Oeni ◽  
Malolactic Enzyme

Exemplar Abstract for Oenococcus oeni (Garvie 1967) Dicks et al. 1995.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Oenococcus Oeni

Exemplar Abstract for Oenococcus oeni (Garvie 1967) Dicks et al. 1995.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Oenococcus Oeni

scholarly journals Use of Yeast Mannoproteins by Oenococcus oeni during Malolactic Fermentation under Different Oenological Conditions

Foods ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1540
Author(s):  
Aitor Balmaseda ◽  
Laura Aniballi ◽  
Nicolas Rozès ◽  
Albert Bordons ◽  
Cristina Reguant
Keyword(s):  
Energy Source ◽  
Nutrient Medium ◽  
Alcoholic Fermentation ◽  
Hydrolytic Activity ◽  
Malolactic Fermentation ◽  
Oenococcus Oeni ◽  
Consumption Patterns ◽  
Inhibitor Compounds

Oenococcus oeni is the main agent of malolactic fermentation in wine. This fermentation takes place after alcoholic fermentation, in a low nutrient medium where ethanol and other inhibitor compounds are present. In addition, some yeast-derived compounds such as mannoproteins can be stimulatory for O. oeni. The mannoprotein concentration in wine depends on the fermenting yeasts, and non-Saccharomyces in particular can increase it. As a result of the hydrolytic activity of O. oeni, these macromolecules can be degraded, and the released mannose can be taken up and used as an energy source by the bacterium. Here we look at mannoprotein consumption and the expression of four O. oeni genes related to mannose uptake (manA, manB, ptsI, and ptsH) in a wine-like medium supplemented with mannoproteins and in natural wines fermented with different yeasts. We observe a general gene upregulation in response to wine-like conditions and different consumption patterns in the studied media. O. oeni was able to consume mannoproteins in all the wines. This consumption was notably higher in natural wines, especially in T. delbrueckii and S. cerevisiae 3D wines, which presented the highest mannoprotein levels. Regardless of the general upregulation, it seems that mannoprotein degradation is more closely related to the fermenting medium.

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