Affiliation:
1. Institut für Mikrobiologie und Weinforschung der Johannes Gutenberg-Universität, Mainz, Germany
Abstract
Three homofermentative (
Lactobacillus plantarum
B38,
L. plantarum
B33,
Pediococcus pentosaceus
B30) and three heterofermentative (
Leuconostoc mesenteroides 39, L. oenos
B70,
Lactobacillus brevis
) lactic acid bacteria were examined for the presence or absence of nicotinamide adenine dinucleotide (NAD)-dependent and NAD-independent
d
- and
l
-lactate dehydrogenases. Two of the six strains investigated,
P. pentosaceus
and
L. oenos
, did not exhibit an NAD-independent enzyme activity capable of reducing dichlorophenol indophenol. The
p
H optima of the lactic dehydrogenases were determined. The NAD-dependent enzymes from homofermentative strains exhibited optima at
p
H 7.8 to 8.8, whereas values from 9.0 to 10.0 were noted for these enzymes from heterofermentative organisms. The optima for the NAD-independent enzymes were between 5.8 and 6.6. The apparent Michaelis-Menten constants determined for both NAD and the substrates demonstrated the existence of a greater affinity for
d
- than
l
-lactic acid. A comparison of the specific NAD-dependent and NAD-independent lactate dehydrogenase activities revealed a direct correlation of the
d/l
ratios of these activities with the type of lactic acid produced during the growth of the organism.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
25 articles.
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