FEMS Microbiology Letters 42 (1987) 213-220 213
Published by Elsevier
FEM 02809
Anabolic role of L-malic acid in Saccharomyces cerevisiae
in anaerobiosis during alcoholic fermentation
J.M. Salmon, F. Vezinhet and P. Barre
Laboratoire de Microbiologie et de Technologie des Fermentations, Institut des Produits de la Vigne, INRA, place Viala,
34060 Montpellier C~dex, France
Received 12 December1986
Accepted 28 February 1987
Key words: Saccharomyces cereoisme; L-Malic acid; Anaerobiosis; Ethanol
1. SUMMARY
In anaerobiosis, pyruvate carboxylase activity
can be greatly reduced by limiting the availability
of biotin to yeast cells. In these conditions an
incorporation of carbon from exogenous L-malic
acid can be observed. The main pathway used for
this anabolic utilization goes through malate dehy-
drogenase and the oxidative reactions of the tri-
carboxylic acid cycle. This anabolic function of
E-malic acid is strongly inhibited by a residual
glucose concentration in the fermenter. This in-
hibition may be due, in this condition, to a higher
intracellular concentration of some negative effec-
tots of malate dehydrogenase such as: 1,6-fructose
diphosphate, glyceraldehyde 3-phosphate, ATP
and ADP.
2. INTRODUCTION
During anaerobiosis, C6-skeleton sugars such as
glucose are catabolized via the glycolysis pathway
Correspondence to: J.M. Salmon, Laboratoire de Microbiologie
et de Technologiedes Fermentations, Institut des Produits de
la Vigne, INRA, place Viala, F-34060 Montpellier C6dex,
France.
to pyruvate, which is decarboxylated to acetalde-
hyde which acts as the terminal electron acceptor.
Ethanol is then the major end-product. This path-
way is mainly orientated to cell energy produc-
tion. A weak part of the intracellular pyruvate
pool is used to prepare building blocks for the
biosynthetic pathways via the subsisting two
branches of the tricarboxylate pathway in
anaerobiosis [1]. An oxidative branch leads to
a-ketoglutarate, serving a purely biosynthetic role,
while a reductive branch leads to succinate and
serves either a biosynthetic or an amphibolic role:
the a-ketoglutarate dehydrogenase step between
these branches is repressed during anaerobiosis
[2-4].
In these conditions, C4-skeleton compounds are
synthetized via pyruvate carboxylase (E.C.6.4.1.1),
the glyoxylic acid shunt being impaired under
anaerobiosis and glucose repression [5-7]. -
After previous results obtained in our labora-
tory [8], we postulated that when the pyruvate
carboxylase activity is greatly reduced, the
degradation of exogenous C4-skeleton compounds
such as L-malic acid could play an anabolic role
and we tried to elucidate the metabolic pathways
involved.
0378-1097/87/$03.50 © 1987 Federation of European MicrobiologicalSocieties
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