Purification and Properties of a Malolactic Enzyme from a Strain of Leuconostoc mesenteroides Isolated from Grapes
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An enzymatic complex able to transform l -malate to l -lactate was obtained from a Leuconostoc mesenteroides strain isolated from grapes. The molecular weight was about 235,000, the isoelectric point was at pH 4.35, and the optimal pH for activity was 5.75. The malolactic activity followed a sequential pattern concerning the involved substrates. At pH values substantially different from the optimum, a positive cooperativity between malate molecules was observed. Oxamate, fructose-1, 6-diphosphate, and l -lactate acted as noncompetitive inhibitors, whereas succinate, citrate, and tartrate isomers produced a competitive inhibition.
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Malic acid decarboxylation to lactic acid is catalyzed by malate decarboxylase (malolactic enzyme) requiring NAD+ and Mn++.
“This reaction is catalysed by the enzyme malate decarboxylase, often referred to as the malolactic enzyme, with the requirement of cofactors NAD + and Mn ++ (Lonvaud-Funel and Strasser de Saad 1982, Caspritz and Radler 1983, Spettoli et al. 1984, Naori et al. 1990, Kunkee 1991) (Figure 10).”
From Yeast and bacterial modulation of wine aroma and flavour (2005) · cites this paper as Lonvaud-Funel and Strasser de Saad 1982
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Yeast and bacterial modulation of wine aroma and flavour
SWIEGERS, J. H., BARTOWSKY, E. J., HENSCHKE, P. A., & PRETORIUS, I. S. (2005) · Australian Journal of Grape and Wine Research · doi:10.1111/j.1755-0238.2005.tb00285.x · Cited by 1,216 · see citing works
Dellaglio, F., Dicks, L. M. T., & Torriani, S. (1995) · The Genera of Lactic Acid Bacteria · doi:10.1007/978-1-4615-5817-0_7 · Cited by 108 · see citing works
- Authors
- Lonvaud-Funel, A., & de Saad, A. M. S.
- Affiliations
- Institut d'Oenologie, Université de Bordeaux II, 33405 Talence, France
- Venue
- Applied and Environmental Microbiology
- Publisher
- American Society for Microbiology
- Published
- 1982-02
- Volume
- 43
- Issue
- 2
- Pages
- 357-361
- ISSN
- 0099-2240 (ISSN-L)
- 1098-5336
- PMC
- PMC241831
- OpenAlex
- W1770848492
- Cited by
- 82
- References
- 0
- Citations by year
- 2024: 2 · 2023: 2 · 2022: 1 · 2021: 4 · 2020: 2 · 2019: 2 · 2018: 2 · 2017: 3 · 2016: 2 · 2015: 3 · 2014: 1 · 2013: 2 · 2012: 2
- FWCI
- 6.66
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Applied and Environmental Microbiology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Fermentation and Sensory Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Keywords
- Leuconostoc mesenteroides, enzyme purification, enzyme kinetics, cooperativity, non-competitive inhibition, competitive inhibition, substrate specificity, isoelectric point, pH optimum
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