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  • Cloning and sequence analysis of the gene encoding Lactococcus lactis malolactic enzyme: relationships with malic enzymes.

Cloning and sequence analysis of the gene encoding Lactococcus lactis malolactic enzyme: relationships with malic enzymes.

FEMS microbiology letters (1994-02-01)
M Denayrolles, M Aigle, A Lonvaud-Funel
ABSTRACT

Malolactic enzyme is the key enzyme in the degradation of L-malic acid by lactic acid bacteria. Using degenerated primers designed from the first 20 N-terminal amino acid sequence of lactococcal malolactic enzyme, a 60-bp DNA fragment containing part of the mleS gene was amplified from Lactococcus lactis in a polymerase chain reaction. This specific probe was used to isolate two contiguous fragments covering the gene as a whole. The 1.9-kb region sequenced contains an open reading frame of 1623 bp, coding a putative protein of 540 amino acids. The deduced amino acid sequence reveals that lactococcal putative protein (Mlep) is highly homologous to the malic enzyme of other organisms. Expression of the mleS gene in Escherichia coli results in malolactic activity.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
L-(−)-Malic acid, ≥95% (titration)
Sigma-Aldrich
L-(−)-Malic acid, ReagentPlus®, ≥99%
Sigma-Aldrich
L-(−)-Malic acid, 97%, optical purity ee: 99% (GLC)
Sigma-Aldrich
L-(−)-Malic acid, BioReagent, suitable for cell culture, suitable for insect cell culture
Supelco
L-(−)-Malic acid, certified reference material, TraceCERT®
Sigma-Aldrich
L-(−)-Malic acid, BioXtra, ≥95%

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