Dataset Information

Draft Genome Sequence of Lactobacillus helveticus Lh 23, Isolated from Natural Whey Starter.

ABSTRACT: Lactobacillus helveticus is a thermophilic lactic acid bacterium that is widely employed as a starter culture for manufacturing several Swiss and Italian hard-cooked cheeses. The sequencing of L. helveticus Lh 23, which consists of 2,100,230?bp with a GC content of 36.5%, reveals industrially useful traits and interesting metabolic pathways.

SUBMITTER: Bertani G

PROVIDER: S-EPMC7484063 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature

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Draft Genome Sequence of Lactobacillus helveticus Lh 23, Isolated from Natural Whey Starter.

Bertani Gaia G Bassi Daniela D Cortimiglia Claudia C Gatti Monica M Cocconcelli Pier Sandro PS Neviani Erasmo E

Microbiology resource announcements 20200910 37

<i>Lactobacillus helveticus</i> is a thermophilic lactic acid bacterium that is widely employed as a starter culture for manufacturing several Swiss and Italian hard-cooked cheeses. The sequencing of <i>L. helveticus</i> Lh 23, which consists of 2,100,230 bp with a GC content of 36.5%, reveals industrially useful traits and interesting metabolic pathways. ...[more]

PMID: 32912904

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Project description:Peptides in the 3-kDa ultrafiltrate of fermented whey protein isolate (WPI) medium could be responsible for the antivirulence activity of Lactobacillus helveticus LH-2 and Lactobacillus acidophilus La-5 against Salmonella Typhimurium. Non-fermented and fermented media containing 5.6% WPI were fractionated at a 3 kDa cut-off and the filtrate was analyzed by mass spectrometry. The non-fermented WPI medium contained 109 milk derived peptides, which originated from ?-casein (52), ?s1-casein (22), ?s2-casein (10), ?-casein (8), and ?-lactoglobulin (17). Most of these peptides were not found in the fermented media, except for 14 peptides from ?-casein and one peptide from ?s2-casein. Database searches confirmed that 39 out of the 109 peptides had established physiological functions, including angiotensin-converting-enzyme (ACE) inhibitory, antioxidant, antimicrobial, or immunomodulating activity. A total of 75 peptides were found in the LH-2 cell free spent medium (CFSM): 54 from ?-casein, 14 from k-casein, 4 from ?-lactoglobulin and 3 from ?s2-casein. From these peptides, 19 have previously been associated with several categories of bioactivity. For La-5 CFSM, a total of 15 peptides were sequenced: 8 from ?-casein, 5 from ?s1-casein, 2 from ?-lactoglobulin. Only 5 of these have previously been reported as having bioactivity. Many of the peptides remaining in the fermented medium would contain low-affinity residues for oligopeptide binding proteins and higher resistance to peptidase hydrolysis. These properties of the sequenced peptides could explain their accumulation after fermentation despite the active proteolytic enzymes of LH-2 and La-5 strains. Down-regulated expression of hilA and ssrB genes in S. Typhimurium was observed in the presence of La-5 and LH-2 CFSM. Downregulation was not observed for the Salmonella oppA mutant strain exposed to the same CFSM used to treat the S. Typhimurium DT104 wild-type strain. This result suggests the importance of peptide transport by S. Typhimurium for down regulation of virulence genes in Salmonella.

Dataset Information

Draft Genome Sequence of Lactobacillus helveticus Lh 23, Isolated from Natural Whey Starter.

Publications

Draft Genome Sequence of Lactobacillus helveticus Lh 23, Isolated from Natural Whey Starter.

Similar Datasets

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