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Cited by 48Probiotics and Fermented FoodsProtein Hydrolysis and Bioactive PeptidesEnzyme Production and Characterization

Growth phase and growth medium effects on the peptidase activities of Lactobacillus helveticus

Kenny, O., FitzGerald, R.J., O’Cuinn, G., Beresford, T., Jordan, K.·2003·International Dairy Journal
DOI 10.1016/s0958-6946(03)00073-6
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Abstract

The effect of growth phase, growth medium and storage conditions on the peptidase activities of Lactobacillus helveticus DPC 4571 were examined. Cell free extracts (CFEs) were prepared from both mid-log and stationary phase cells grown in either 10% (w/v) reconstituted skim milk (RSM) or MRS pH 5.4 broth. In general, Lb. helveticus DPC 4571 was found to possess a broad range of aminopeptidase, dipeptidase, tripeptidase, endopeptidase and proline-specific peptidase activities. The stability of these peptidase activities in a CFE of Lb. helveticus DPC 4571 stored at 4°C was variable. The specific activities of the majority of these peptidases were significantly (P<0.05) influenced by both growth phase and growth medium. Cells grown to mid-log phase in RSM were found to have the highest level of peptidase activity.

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Crossref · 10.1016/s0958-6946(03)00073-6

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  • The proteolytic system of L. helveticus and the majority of LAB consists of proteinases, intracellular peptidases, and specific transport proteins.

    “The proteolytic system of L. helveticus and the majority of LAB consists of proteinases which initially cleave caseins to large peptides, peptidases (intracellular), which further degrade these peptides to small peptides and amino acids, and specific transport proteins which transport amino acids and peptides across the cytoplasmic membrane (Kenny et al., 2003).”

    From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Kenny et al., 2003

  • Up until 2003 just 11 peptidases were known to be part of the proteolytic system of L. helveticus: two proline-specific endopeptidases, PepE and PepO; a tripeptidase PepT; four aminopeptidases, PepX, PepI, PepQ, and PepR; and four dipeptidases, PepD, PepV, PepC, and PepN.

    “Up until 2003 just 11 peptidases were known to be part of the proteolytic system of L. helveticus: two proline-specific endopepeptidases, PepE and PepO; a tripeptidase PepT; four aminopeptidases, PepX, PepI, PepQ, and PepR; and four dipeptidases, PepD, PepV, PepC, and PepN (Christensen et al., 1999; Savijoki and Palva, 2000; Kenny et al., 2003; Pan and Tanokur, 2004).”

    From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Kenny et al., 2003

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Authors
Kenny, O., FitzGerald, R. J., O’Cuinn, G., Beresford, T., & Jordan, K.
Affiliations
  • Teagasc - The Irish Agriculture and Food Development Authority (IE)
  • University of Limerick (IE)
  • Galway-Mayo Institute of Technology (IE)
Corresponding author
Jordan, K.
ORCID
Venue
International Dairy Journal
Publisher
Elsevier BV
Published
2003-01
Volume
13
Issue
7
Pages
509-516
ISSN
0958-6946 (ISSN-L)
DOI
10.1016/s0958-6946(03)00073-6
OpenAlex
W2063320704
Cited by
47
References
37
Citations by year
2026: 2 · 2025: 2 · 2023: 2 · 2022: 3 · 2021: 4 · 2020: 1 · 2019: 2 · 2018: 4 · 2017: 2 · 2015: 2 · 2014: 3 · 2013: 1 · 2012: 1
FWCI
3.27
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
International Dairy Journal (publishedVersion)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
Keywords
Lactobacillus helveticus, proteolytic activity, growth phase, culture media, reconstituted skim milk, MRS broth, aminopeptidase, dipeptidase, tripeptidase, endopeptidase, cell-free extracts, enzyme stability, storage conditions, probiotic bacteria

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