The DOI matches its Crossref record; 258 of the 259 references it cites were found in a registry or an index.
Peptidases and amino acid catabolism in lactic acid bacteria
Abstract
The conversion of peptides to free amino acids and their subsequent utilization is a central metabolic activity in prokaryotes. At least 16 peptidases from lactic acid bacteria (LAB) have been characterized biochemically and/or genetically. Among LAB, the peptidase systems of Lactobacillus helveticus and Lactococcus lactis have been examined in greatest detail. While there are homologous enzymes common to both systems, significant differences exist in the peptidase complement of these organisms. The characterization of single and multiple peptidase mutants indicate that these strains generally exhibit reduced specific growth rates in milk compared to the parental strains. LAB can also catabolize amino acids produced by peptide hydrolysis. While the catabolism of amino acids such as Arg, Thr, and His is well understood, few other amino acid catabolic pathways from lactic acid bacteria have been characterized in significant detail. Increasing research attention is being directed toward elucidating these pathways as well as characterizing their physiological and industrial significance.
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In the citing paper
“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 Christensen et al., 1999
In the citing paper
“Pathways for the catabolism of tryptophan (a), phenylalanine (b) and tyrosine (c), by starter, adjunct and non-starter bacteria (modified from [24]).”
From Biochemical pathways for the production of flavour compounds in cheeses during ripening: A review (2000) · cites this paper as [24]
In the citing paper
“Three different Asp catabolic pathways have been reported [24]; however, the details and distribution of these pathways are still not well understood.”
From Biochemical pathways for the production of flavour compounds in cheeses during ripening: A review (2000) · cites this paper as [24]
In the citing paper
“A common pathway in LAB for the catabolism of Arg results in the conversion of 1 mol of Arg into 2 mol of ammonia and 1 mol each of ornithine, carbon dioxide, and ATP [24].”
From Biochemical pathways for the production of flavour compounds in cheeses during ripening: A review (2000) · cites this paper as [24]
In the citing paper
“The reported pathways of Glu catabolism produce α-ketoglutarate by the action of an aminotransferase or dehydrogenase, or γ-aminobutyrate (GABA) by the action of a decarboxylase [24].”
From Biochemical pathways for the production of flavour compounds in cheeses during ripening: A review (2000) · cites this paper as [24]
In the citing paper
“Catabolism of branched-chain amino acids is typically associated with the generation of compounds having a detrimental effect on product aroma or flavour in the production of fermented dairy products [24].”
From Biochemical pathways for the production of flavour compounds in cheeses during ripening: A review (2000) · cites this paper as [24]
In the citing paper
“Amino acids can be catabolised by several reactions: deamination, decarboxylation, oxidative desamination, transamination and elimination [14,55,67].”
From Production of cheese flavour compounds derived from amino acid catabolism by Propionibacterium freudenreichii (2002) · cites this paper as [14]
In the citing paper
“In general, branched-chain acids appear to be more prevalent in Swisstype cheeses and some Italian cheeses than in semi-hard cheese like Cheddar, Edam and Gouda [9,14,17,55].”
From Production of cheese flavour compounds derived from amino acid catabolism by Propionibacterium freudenreichii (2002) · cites this paper as [14]
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Scolari, G., & Vescovo, M. (2004) · European Food Research and Technology · doi:10.1007/s00217-004-1066-3
Meli, F. (2013) · DSpaceUnipr (University of Parma)
Hu, K. (2009) · University Library - University of Saskatchewan (University of Saskatchewan)
Production of functional food, Fruit ravioli with antihypertensive peptides
Acharya, P., & Jayabalan, R. (2014)
Milk casein-derived tripeptides : A special focus on blood pressure and vascular function
Ehlers, P. I. (2010) · Työväentutkimus Vuosikirja
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Metadata
- Authors
- Christensen, J. E., Dudley, E. G., Pederson, J. A., & Steele, J. L.
- Affiliations
- University of Wisconsin–Madison (US)
- Corresponding author
- Steele, James L.
- Venue
- Antonie van Leeuwenhoek
- Published
- 1999-11
- Volume
- 76
- Issue
- 1-4
- Pages
- 217-246
- ISSN
- 0003-6072 (ISSN-L)
- 1572-9699
- OpenAlex
- W1563027263
- Cited by
- 630
- References
- 259
- Citations by year
- 2026: 5 · 2025: 18 · 2024: 18 · 2023: 18 · 2022: 23 · 2021: 14 · 2020: 25 · 2019: 13 · 2018: 20 · 2017: 30 · 2016: 24 · 2015: 24 · 2014: 28 · 2013: 20 · 2012: 32
- FWCI
- 46.32
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Antonie van Leeuwenhoek (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- proteolytic enzymes, amino acid catabolism, lactic acid bacteria, Lactobacillus helveticus, Lactococcus lactis, peptide hydrolysis, amino acid utilization, arginine catabolism, histidine catabolism
- MeSH terms
- Amino Acid Sequence, Amino Acids, Animals, Gram-Positive Bacteria, Lactobacillus, Peptide Hydrolases, Substrate Specificity, Lactic Acid
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