Výskumný ústav potravinársky

Brežná, B. – Drahovská, H. – Holbíková, E. – Kuchta, T.
Sequencing and analysing the genome of Lactiplantibacillus plantarum DSM 12028 in search of extracellular lipases
Journal of Food and Nutrition Research, 63, 2024, č. 4, s. 352-356

Barbara Brežná, Department of Microbiology and Molecular Biology, Food Research Institute, National Agricultural and Food Centre, Priemyselná 4, 82475 Bratislava, Slovakia. E-mail: barbara.brezna@nppc.sk

Short communication
Received 14 October 2024; 1st revised 27 November 2024; accepted 29 November 2024; published online 2 December 2024.

Súhrn: Lipases are enzymes whose activity often positively contributes to the development of the characteristic aroma during cheese ripening. They may originate from microorganisms present in milk or from starter cultures. This study attempted to identify four extracellular lipases of Lactiplantibacillus plantarum (formerly Lactobacillus plantarum), which were previously partially purified and characterised by a different research group two decades ago, providing the N-terminal protein sequences. The genome of Lb. plantarum DSM 12028 was sequenced in the current work and the protein matches for the sequenced fragments were searched for. The matches were correctly located at proteins’ N-termini, if the removal of the pre-protein domain was considered, to simulate the protein maturation by Signal peptidase I. However, the identified proteins are peptidoglycan hydrolases rather than lipases. The lipase activity observed in the previous study might have been caused by different proteins co-eluted with the peptidoglycan hydrolases, but substrate specificity should be experimentally verified for definitive conclusion. The genome was searched for other extracellular hydrolase genes, possibly lipases or esterase, resulting in 17 candidates. Additionally, the genomic sequence of the strain will be valuable for research teams investigating its potential as a probiotic strain.

Kľúčové slová: cheese; lactic acid bacteria; cell wall; lipase; esterase; transglycosylase; muropeptidase

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