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Superior esterolytic activity in environmental Lactococcus lactis strains is linked to the presence of the SGNH hydrolase family of esterases

Abstract : We investigated the esterolytic activity of dairy- and environment-derived Lactococcus lactis strains through a quantitative esterase assay based on hydrolysis of p-nitrophenyl dodecanoate (PNP). In general, environmental L. lactis strains had higher esterolytic activity than dairy strains. Comparative genome analysis revealed the presence of an open reading frame related to esterolytic activity in the environmental strain L. lactis DPC6855 (from corn), encoding the predicted product SGNH/GDSL hydrolase family protein. The 1,287-bp gene encodes a 428-amino acid SGNH/GDSL hydrolase. The presence of this gene in most of the environment-derived strains was established by PCR; the gene was not found in the genome of L. lactis DPC6853 or in genomes of L. lactis strains from dairy sources, suggesting a possible correlation between the SGNH hydrolase family and higher esterolytic activity. This work provides further evidence of more diverse genotypic and phenotypic traits in environmental compared with dairy L. lactis strains.
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https://hal.inrae.fr/hal-03028324
Contributor : Anne Thierry <>
Submitted on : Friday, November 27, 2020 - 3:18:35 PM
Last modification on : Wednesday, December 2, 2020 - 3:37:22 AM
Long-term archiving on: : Sunday, February 28, 2021 - 8:01:18 PM

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Desirée Román Naranjo, Michael Callanan, Anne Thierry, Olivia Mcauliffe. Superior esterolytic activity in environmental Lactococcus lactis strains is linked to the presence of the SGNH hydrolase family of esterases. JDS Communications, American Dairy Science Association, 2020, 1, pp.25-28. ⟨hal-03028324⟩

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