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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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]
Citations
Cites
Items 201–258 of 258
Purification and Characterization of a Dipeptidase from Lactobacillus helveticus SBT 2171
Tan, P., Sasaki, M., Bosman, B. W., & Iwasaki, T. (1995) · Applied and Environmental Microbiology · doi:10.1128/aem.61.9.3430-3435.1995 · Cited by 30
Tsakalidou, E., & Kalantzopoulos, G. (1992) · Journal of Applied Bacteriology · doi:10.1111/j.1365-2672.1992.tb01828.x · Cited by 29
Sasaki, M., Bosman, B. W., & Tan, P. S. T. (1996) · Microbiology · doi:10.1099/00221287-142-4-799 · Cited by 29
Roudot-Algaron, F., & Yvon, M. (1998) · Le Lait · doi:10.1051/lait:199814 · Cited by 29
Histamine and Histamine-Producing Bacteria in Retail Swiss and Low-Salt Cheeses
Stratton, J., Hutkins, R. W., Sumner, S. S., & Taylor, S. L. (1992) · Journal of Food Protection · doi:10.4315/0362-028x-55.6.435 · Cited by 29
Roig-Sagués, A. X., Hernández-Herrero, M. M., López-Sabater, E. I., Jerez, J. J. R., & Mora-Ventura, M. T. (1997) · Letters in Applied Microbiology · doi:10.1046/j.1472-765x.1997.00223.x · Cited by 28
Lerch, H.-P., Frank, R., & Collins, J. F. (1989) · Gene · doi:10.1016/0378-1119(89)90112-1 · Cited by 28
Degradation of abnormal proteins in peptidase-deficient mutants of Salmonella typhimurium
Miller, C. G., & Green, L. (1981) · Journal of Bacteriology · doi:10.1128/jb.147.3.925-930.1981 · Cited by 28
Biosynthesis of the Aspartate Family of Amino Acids
Paulus, H. (2014) · ASM Press eBooks · doi:10.1128/9781555818388.ch18 · Cited by 27
Sahlstr�m, S., Chrzanowska, J., & S�rhaug, T. (1993) · Applied and Environmental Microbiology · doi:10.1128/aem.59.9.3076-3082.1993 · Cited by 27
Shao, W., Yüksel, G. U., Dudley, E. G., Parkin, K. L., & Steele, J. L. (1997) · Applied and Environmental Microbiology · doi:10.1128/aem.63.9.3438-3443.1997 · Cited by 26
Self-citationHuynh, Q. K., Recsei, P. A., Vaaler, G. L., & Snell, E. E. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43222-4 · Cited by 26
Bacon, C. L., Jennings, P. V., Fhaoláin, Í. N., & O’Cuinn, G. (1994) · International Dairy Journal · doi:10.1016/0958-6946(94)90022-1 · Cited by 26
Bockelmann, W., Beuck, H.-P., Lick, S., & Heller, K. J. (1995) · International Dairy Journal · doi:10.1016/0958-6946(95)00029-3 · Cited by 25
Desmazeaud, M., & Zevaco, C. (1977) · annales de biologie animale biochimie biophysique · doi:10.1051/rnd:19770608 · Cited by 24
TonB-dependent iron supply inSalmonellaby α-ketoacids and α-hydroxyacids
Kingsley, R. A., Rabsch, W., Roberts, M., Reissbrodt, R., & WILLIAMS, P. H. (1996) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1996.tb08316.x · Cited by 23
Purification and Properties of Intracellular Proteinase from Streptococcus cremoris
Ohmiya, K., & Sato, Y. (1975) · Applied Microbiology · doi:10.1128/am.30.5.738-745.1975 · Cited by 23
Purification and characterization of an aminopeptidase from Lactobacillus casei subsp. rhamnosus S93
Arora, G., & Lee, B. H. (1994) · Biotechnology and Applied Biochemistry · doi:10.1111/j.1470-8744.1994.tb00293.x · Cited by 22
The molecular cloning, sequence and expression of the hdcB gene from Lactobacillus 30A
Copeland, W. C., Domena, J. D., & Robertas, J. D. (1989) · Gene · doi:10.1016/0378-1119(89)90492-7 · Cited by 22
Lactobacillus delbrueckii subsp. lactis DSM7290 pepG gene encodes a novel cysteine aminopeptidase
Klein, J. R., Schick, J., Henrich, B., & Plapp, R. (1997) · Microbiology · doi:10.1099/00221287-143-2-527 · Cited by 22
St-PepA, a Streptococcus thermophilus aminopeptidase with high specificity for acidic residues
Rul, F., Gripon, J. C., & Monnet, V. (1995) · Microbiology · doi:10.1099/13500872-141-9-2281 · Cited by 22
Enzymic activities associated with lactobacilli in dairy products.
Hickey, M. W., Hillier, A. J., & Jago, G. R. (1983) · Australian Journal of Dairy Technology · Cited by 22
NUTRITIONAL REQUIREMENTS OF LACTOBACILLUS 30a FOR GROWTH AND HISTIDINE DECARBOXYLASE PRODUCTION
Guirard, B. M., & Snell, E. E. (1964) · Journal of Bacteriology · doi:10.1128/jb.87.2.370-376.1964 · Cited by 21
Tsakalidou, E., Dalezios, I., Georgalaki, M. D., & Kalantzopoulos, G. (1993) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(93)77549-9 · Cited by 21
Characterization of an intracellular oligopeptidase from Lactobacillus paracasei
Tobiassen, R. O., Sørhaug, T., & Stepaniak, L. (1997) · Applied and Environmental Microbiology · doi:10.1128/aem.63.4.1284-1287.1997 · Cited by 21
Volatile acids of Swiss cheese
Patton, S. (1964) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(64)88772-5 · Cited by 20
Bockelmann, W., Hoppe-Seyler, T., & Heller, K. J. (1996) · International Dairy Journal · doi:10.1016/0958-6946(95)00023-2 · Cited by 20
Fernández-Esplá, M. D., & Martín-Hernández, M. C. (1997) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(97)76078-8 · Cited by 20
Morel, F., Gilbert, C., Geourjon, C., Frot-Coutaz, J. P., Portalier, R. C., & Atlan, D. (1999) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(98)00264-7 · Cited by 20
Varmanen, P., Steele, J. L., & Palva, A. (1996) · Microbiology · doi:10.1099/00221287-142-4-809 · Cited by 20
Self-citationLloyd, D., Lauritsen, F. R., & Degn, H. (1991) · Journal of General Microbiology · doi:10.1099/00221287-137-7-1743 · Cited by 20
Stucky, K., Schick, J., Klein, J. ⁄. R. R., Henrich, B., & Plapp, R. (1996) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1996.tb08026.x · Cited by 20
Misono, H., Goto, N., & Nagasaki, S. (1985) · Agricultural and Biological Chemistry · doi:10.1080/00021369.1985.10866676 · Cited by 19
Rantanen, T., & Palva, A. (1997) · Microbiology · doi:10.1099/00221287-143-12-3899 · Cited by 18
Threonine aldolase activity in yogurt bacteria as determined by headspace gas chromatography
Wilkins, D. W., Schmidt, R. H., & Kennedy, L. B. (1986) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00067a040 · Cited by 18
Purification and partial characterization of a tripeptidase from Pediococcus pentosaceus K9.2
Simitsopoulou, M., Vafopoulou, A., Choli‐Papadopoulou, T., & Alichanidis, E. (1997) · Applied and Environmental Microbiology · doi:10.1128/aem.63.12.4872-4876.1997 · Cited by 18
Catalytic properties of the cysteine aminopeptidase PepC, a bacterial bleomycin hydrolase
Mistou, M., & Gripon, J. C. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(97)00185-4 · Cited by 18
Marranzini, R. M., Schmidt, R. H., Shireman, R. B., Marshall, M. R., & Cornell, J. A. (1989) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(89)79217-1 · Cited by 17
Mistou, M., Rigolet, P., Chapot, M.-P., Nardi, M., Gripon, J. C., & Brunie, S. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1215 · Cited by 17
Characterization of the Aminopeptidase System fromLactobacillus caseiSubsp.caseiIFPL 731
de Palencia, P. F., Peláez, C., & Martín-Hernández, M. C. (1997) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf9703213 · Cited by 16
de Palencia, P. F., de Felipe, F. L., Requena, T., & Peláez, C. (2000) · European Food Research and Technology · doi:10.1007/s002170000203 · Cited by 15
Feil, I., Hendle, J., & Schomburg, D. (1997) · Protein Engineering Design and Selection · doi:10.1093/protein/10.3.255 · Cited by 15
Mata, L., Erra-Pujada, M., Gripon, J. C., & Mistou, M. (1997) · Biochemical Journal · doi:10.1042/bj3280343 · Cited by 15
Wohlrab, Y., & Bockelmann, W. (1994) · International Dairy Journal · doi:10.1016/0958-6946(94)90056-6 · Cited by 13
Lian, W., Wu, D., Konings, W. N., Mierau, I., & Hersh, L. B. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0372 · Cited by 13
Yoshpe-Besancon, I., Gripon, J. C., & RIBADEAU‐DUMAS, B. (1994) · Biotechnology and Applied Biochemistry · doi:10.1111/j.1470-8744.1994.tb00310.x · Cited by 13
Purification and Characterization of an Endopeptidase from Propionibacterium freudenreichii
Tobiassen, R. O., Pripp, A. H., Stepaniak, L., & Sørhaug, T. (1996) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(96)76587-6 · Cited by 12
Deletion variants of l ‐hydroxyisocaproate dehydrogenase
Feil, I., Lerch, H.-P., & Schomburg, D. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb19062.x · Cited by 11
Chich, J., Rigolet, P., Nardi, M., Gripon, J. C., RIBADEAU‐DUMAS, B., & Brunie, S. (1995) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340230216 · Cited by 11
Aspartate metabolism in Lactobacillus murinus CNRS 313. I. Aspartase.
Rollán, G., de Nadra, M. C. M., Holgado, A. A. P. D. R., & OLIVER, G. (1985) · The Journal of General and Applied Microbiology · doi:10.2323/jgam.31.403 · Cited by 10
Stepaniak, L., Tobiassen, R. O., Chukwu, I., Pripp, A. H., & Sørhaug, T. (1998) · International Dairy Journal · doi:10.1016/s0958-6946(98)00016-8 · Cited by 8
Peptidases and growth of Lactococcus lactis in milk
Mierau, I., Kunji, E. R. S., Venema, G., Poolman, B., & Kok, J. (1996) · Le Lait · doi:10.1051/lait:19961-23 · Cited by 8
Aspartate aminotransferase ofLactobacillus murinus
Rollán, G., de Nadra, M. C. M., Holgado, A. P. D. R., & Oliver, G. (1988) · Folia Microbiologica · doi:10.1007/bf02925842 · Cited by 6
Stepaniak, L., Gobbetti, M., Pripp, A. H., & Sørhaug, T. (1998) · CINECA IRIS Institutional Research Information System (University of Bari Aldo Moro) · Cited by 6
Houbart, V., RIBADEAU‐DUMAS, B., & Chich, J. (1995) · HAL · Cited by 5
Purification and characterisation of an aminopeptidase from Lactobacillus curvatus DPC2024
Magboul, A. A. A., & McSweeney, P. L. H. (1998) · Australian Journal of Dairy Technology · Cited by 2
Gummalla, S. (2021) · Digital Commons - USU (Utah State University) · doi:10.26076/b85f-db74 · Cited by 2
Dynamic headspace analysis of volatile compounds of Cheddar and Swiss cheeses during ripening.
Ts, Y., & Db, M. (1993) · Developments in food science · Cited by 2
Research works printed but not linked: 17
- Biede SL, Paulsen PV, Hammond EG & Glatz BA (1979) The flavor of Swiss cheese. In: Underkofler LA (Ed) Development in Industrial Microbiology, (pp 203-210). Society for Industrial Microbiology, Arlington, VA
- Bockelmann W, Gollan V & Heller KJ (1997) Purification of a second tripeptidase from Lactobacillus delbrueckii subsp. bulgaricus B14. Milchwissenschaft 52: 500-503
- Christensen JE & Steele JL (1996) Characterization of peptidase-deficient Lactobacillus helveticus CNRZ32 derivatives. Fifth Symposium on Lactic Acid Bacteria, Veldhoven, The Netherlands
- Christensen JE & Steele JL (1998a) Hydrolysis of casein derived peptides by peptidase-deficient Lactobacillus helveticus CNRZ32 derivatives. Joint Meeting of the American Dairy Science Association and the American Society of Animal Science. Journal of Dairy Science, Denver, Colorado, USA.
- Desmazeaud MJ & Zevaco C (1979) Isolation and general properties of two intracellular amino peptidases of Streptococcus diacetylactis. Milchwissenschaft 34: 606-610
- Gummalla S & Broadbent JR (1996) Indole production by Lactobacillus ssp. in cheese: a possible role for tryptophanase. J. Dairy Sci. 79(Suppl. 1): 101
- Guthrie BD (1993) Influence of cheese-related microflora on the production of unclean-flavored aromatic amino acid metabolites in Cheddar cheese. Ph.D thesis, University of Wisconsin-Madison
- Kaminogawa S, Azuma N, Hwang IK, Suzuki Y & Yamauchi K (1984) Isolation and characterization of a prolidase from Streptococcus cremoris H61. Agric. Biol. Chem. 48: 3035-3040
- Kong Y, Strickland M & Broadbent JR (1996) Tyrosine and phenylalanine catabolism by Lactobacillus casei flavor adjuncts: biochemistry and implications in cheese flavor. J. Dairy Sci. 79(Suppl. 1): 101
- Law BA (1981) The formation of aroma and flavor compounds in fermented dairy products. Dairy Sci. Abstr. 43: 143
- Manca de Nadra MC, Pese de Ruiz Holgado AA & Oliver G (1982) Arginine dihydrolase activity in lactic acid bacteria. Milchwissenschaft 37: 669-670
- Manca De Nadra MC, Raya RR, Pesce De Ruiz Holgado A & Oliver G (1987) Isolation and properties of threonine aldolase of Lactobacillus bulgaricus YOP12. Milchwissenschaft 42: 92-94
- Reiter B & Oram JD (1962) Nutritional studies on cheese starters. I. Vitamin and amino acid requirements of single strain starters. J Dairy Res. 29: 63-77
- Shankar PA (1977) Interrelationships of Streptococcus thermophilus and Lactobacillus bulgaricus in yoghurt culture. Thesis, University of Reading, Reading, UK
- Stepaniak L, Gobbetti M & Sorhaug T (1998b) Isolation and characterization of high molecular mass endopeptidase complex from Lactococcus lactis. Milchwissenschaft 53: 255-259
- Yan TR, Lin MZ, Lin MJ & Sun BJ (1991) Purification and characterization of an X-prolyl-dipeptidyl aminopeptidase from Streptococcus cremoris nTR. J. Chin. Biochem. Soc. 20: 21-32
- Zoon P & Allersma D (1996) Eye and crack formation in cheese by carbon dioxide from decarboxylation of glutamic acid. Neth. Milk Dairy J. 50: 309-318
Cited by
Sorted by citations
Bioactive peptides: Production and functionality
Korhonen, H. J. T., & Pihlanto, A. (2006) · International Dairy Journal · doi:10.1016/j.idairyj.2005.10.012 · Cited by 1,822
Complete genome sequence of Lactobacillus plantarum WCFS1
Kleerebezem, M., Boekhorst, J., van Kranenburg, R., Molenaar, D., Kuipers, O. P., Leer, R., Tarchini, R., Peters, S. A., Sandbrink, H. M., Fiers, M. W. E. J., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0337704100 · Cited by 1,472
Biochemical pathways for the production of flavour compounds in cheeses during ripening: A review
McSweeney, P. L. H., & Sousa, M. J. (2000) · Le Lait · doi:10.1051/lait:2000127 · Cited by 1,266
Yeast and bacterial modulation of wine aroma and flavour
SWIEGERS, J. H., BARTOWSKY, E. J., HENSCHKE, P. A., & PRETORIUS, I. S. (2005) · Australian Journal of Grape and Wine Research · doi:10.1111/j.1755-0238.2005.tb00285.x · Cited by 1,216
The Complete Genome Sequence of the Lactic Acid Bacterium Lactococcus lactis ssp. lactis IL1403Preprint
Bolotin, A., Wincker, P., Mauger, S., Jaillon, O., Malarme, K., Weissenbach, J., Ehrlich, S. D., & Sorokin, A. (2001) · Genome Research · doi:10.1101/gr.169701 · Cited by 1,161
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
