Gene cloning, sequencing, and inactivation of the branched-chain aminotransferase of Lactococcus lactis LM0230

Article Abstract:

Research has been conducted on the branched-chain Lactococcus lactis aminotansferase gene. The identification of this gene on a chromosomal insert by complementation in Escherichia coli is described.

Analysis, Escherichia coli, Cloning, Chromosomes, Aminotransferases, Transaminases, Microbiological research

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Lactococcus lactis LM1230 contains a single aminotransferase involved in aspartate biosynthesis, which is essential for growth in milk

Article Abstract:

It appears that only one lactococcal ATase takes part in the conversion of oxaloacetate to Asp, the Asp biosynthesis of which is necessary for growth of Lactococcus lactis LM0230 in milk. The aspartate ATase gene (aspC) from L. lactis LM0120 was cloned by complementation into Escherichia coli DL30. One chromosomal fragment putatively encoding apsC was partially sequenced.

Physiological aspects, Bacteria, Biosynthesis, Cytochemistry, Amino acids, Milk, Dairy bacteriology, Amino acid synthesis, Aspartate aminotransferase

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Biochemical and molecular characterization of PepR, a dipeptidase, from Lactobacillus helveticus CNRZ32

Article Abstract:

Microbiological research shows that a dipeptidase enzyme with prolinase activity exists in the lactic acid bacteria Lactobacillus helveticus CNRZ32 that is a serine-dependent protease. The enzyme does not appear to be necessary for milk acidification although its absence impacts dipetidase activity. The enzyme has an isoelectric point of 4.5.

Lactobacillus, Lactic acid, Lactic acidosis

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