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The physiology and biochemistry of the proteolytic system in lactic acid bacteria
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The inability of lactic acid bacteria to synthesize many of the amino acids required for protein synthesis necessitates the active functioning of a proteolytic system in those environments where protein constitutes the main nitrogen source. Biochemical and genetic analysis of the pathway by which exogenous proteins supply essential amino acids for growth has been one of the most actively investigated aspects of the metabolism of lactic acid bacteria especially in those species which are of importance in the dairy industry, such as the lactococci. Much information has now been accumulated on individual components of the proteolytic pathway in lactococci, namely, the cell envelope proteinase(s), a range of peptidases and the amino acid and peptide transport systems of the cell membrane. Possible models of the proteolytic system in lactococci can be proposed but there are still many unresolved questions concerning the operation of the pathway in vivo. This review will examine current knowledge and outstanding problems regarding the proteolytic system in lactococci and also the extent to which the lactococcal system provides a model for understanding proteolysis in other groups of lactic acid bacteria.
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“As lactic acid synthesis through fermentation is associated to cell growth, there is no formation of product if the medium does not have an adequate concentration of nitrogen in order to promote this growth (Pritchard and Coolbear, 1993).”
From Response surface optimization of D(-)-lactic acid production by Lactobacillus SMI8 using corn steep liquor and yeast autolysate as an alternative nitrogen source (2009) · cites this paper as Pritchard and Coolbear, 1993
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Self-citationAminopeptidase Profiles of Lactic Streptococci
Kaminogawa, S., Ninomiya, T., & YAMAUCHI, K. (1984) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(84)81604-5 · Cited by 44
Monnet, V., Ley, J. P., & González, S. (1992) · International Journal of Biochemistry · doi:10.1016/0020-711x(92)90004-k · Cited by 44
Isolation and characterization of a prolidase from Streptococcus cremoris H61.
Kaminogawa, S., Azuma, N., Hwang, I.-K., Suzuki, Y., & YAMAUCHI, K. (1984) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.48.3035 · Cited by 43
Deletion analysis of the proteinase gene of Streptococcus cremoris Wg2
Kok, J., Hill, D., Haandrikman, A. J., de Reuver, M. J., Laan, H., & Venema, G. (1988) · Applied and Environmental Microbiology · doi:10.1128/aem.54.1.239-244.1988 · Cited by 42
Nas, H., & Nissen-Meyer, J. (1992) · Journal of General Microbiology · doi:10.1099/00221287-138-2-313 · Cited by 42
Coolbear, T., Reid, J. R., & PRITCHARD, G. G. (1992) · Applied and Environmental Microbiology · doi:10.1128/aem.58.10.3263-3270.1992 · Cited by 41
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Kolstad, J., & Law, B. A. (1985) · Journal of Applied Bacteriology · doi:10.1111/j.1365-2672.1985.tb01484.x · Cited by 39
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Khalid, N. M., El Soda, M., & Marth, E. H. (1991) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(91)78140-x · Cited by 37
Ezzat, N., Zevaco, C., Soda, M. E., & Gripon, J. C. (1987) · HAL · Cited by 37
Wohlrab, Y., & Bockelmann, W. (1993) · International Dairy Journal · doi:10.1016/0958-6946(93)90083-c · Cited by 36
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Muset, G., Monnet, V., & Gripon, J. C. (1989) · Journal of Dairy Research · doi:10.1017/s0022029900029344 · Cited by 36
Transport of basic amino acids by membrane vesicles of Lactococcus lactis
Driessen, A. J. M., van Leeuwen, C., & Konings, W. N. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.3.1453-1458.1989 · Cited by 35
Location and characterization of aminopeptidase N in Lactococcus lactis subsp. cremoris HP
Exterkate, F. A., de Jong, M., de Veer, G. J. C. M., & Baankreis, R. (1992) · Applied Microbiology and Biotechnology · doi:10.1007/bf00174202 · Cited by 34
Peptidases of Lactobacillus casei and L. plantarum
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Desmazeaud, M., & Zevaco, C. (1976) · annales de biologie animale biochimie biophysique · doi:10.1051/rnd:19760608 · Cited by 31
Ornithine transport and exchange in Streptococcus lactis
Thompson, J. F. (1987) · Journal of Bacteriology · doi:10.1128/jb.169.9.4147-4153.1987 · Cited by 30
Dipeptide utilization by starter streptococci
Law, B. A. (1977) · Journal of Dairy Research · doi:10.1017/s0022029900020239 · Cited by 30
Tsakalidou, E., & Kalantzopoulos, G. (1992) · Journal of Applied Bacteriology · doi:10.1111/j.1365-2672.1992.tb01828.x · Cited by 29
Gene Organization and Expression in Mesophilic Lactic Acid Bacteria
de Vos, W. M., Vos, P., Simons, G., & David, S. (1989) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(89)79503-5 · Cited by 28
Laan, H., Smid, E. J., de Leij, L., Schwander, E., & Konings, W. N. (1988) · Applied and Environmental Microbiology · doi:10.1128/aem.54.9.2250-2256.1988 · Cited by 28
Optimal growth of Streptococcus cremoris HP in milk is related to β- and ϰ-casein degradation
Exterkate, F. A., & de Veer, G. J. C. M. (1987) · Applied Microbiology and Biotechnology · doi:10.1007/bf00253321 · Cited by 25
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Crow, V. L., Holland, R., & Coolbear, T. (1993) · International Dairy Journal · doi:10.1016/0958-6946(93)90103-7 · Cited by 24
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ABBOUDI, M. E., Soda, M. E., Pandian, S. K., et al. (1992) · International Journal of Food Microbiology · doi:10.1016/0168-1605(92)90138-s · Cited by 22
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El‐Shafei, H., El‐Soda, M., & Ezzat, N. (1990) · Journal of Food Protection · doi:10.4315/0362-028x-53.2.165 · Cited by 18
Peptidase activity of non-starter lactobacilli.
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The cell-bound proteinase system of Lactobacillus casei — purification and characterization
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Proteolytic activity of crude cell‐free extract of Lactobacillus casei and Lactobacillus plantarum
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Peptide-hydrolysing enzymes of Pediococcus species
Bhowmik, T., & Marth, E. H. (1990) · Microbios · Cited by 14
Extracellular proteinases from Micrococcus GF : II. Isolation and characterization
de Fernando, G. D. G., & Fox, P. F. (1991) · Le Lait · doi:10.1051/lait:1991329 · Cited by 14
Prasad, R., Malik, R. K., & Mathur, D. K. (1986) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(86)80450-7 · Cited by 14
Bhowmik, T., & Marth, E. H. (1989) · Systematic and Applied Microbiology · doi:10.1016/s0723-2020(89)80046-3 · Cited by 13
Proteinase genes of cheese starter cultures
Kok, J. (1991) · Biochemical Society Transactions · doi:10.1042/bst0190670 · Cited by 13
Flavour peptides: the potential role of Lactococcal peptidases in their production
Mulholland, F. (1991) · Biochemical Society Transactions · doi:10.1042/bst0190685 · Cited by 11
Extracellular proteinase fromEnterococcus faecalis subsp.liquefaciens
de Fernando, G. D. G., Hernández, P. E., Burgos, J., et al. (1991) · Folia Microbiologica · doi:10.1007/bf02884061 · Cited by 10
Production, processing, and engineering of the Lactococcus lactis SK11 proteinase.
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From casein to cheese: The role ofLactococcus lactis
Konings, W. N., Smid, E. J., Laan, H., & Driessen, A. J. M. (1991) · Food Biotechnology · doi:10.1080/08905439109549809 · Cited by 6
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THE BIOCHEMICAL, GENETIC AND PHYSIOLOGICAL-PROPERTIES OF AMINOPEPTIDASE-N FROM LACTOCOCCUS-LACTIS
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Metadata
- Authors
- Pritchard, G. G., & Coolbear, T.
- Affiliations
- Massey University (NZ)
- Venue
- FEMS Microbiology Reviews
- Publisher
- Oxford University Press (OUP)
- Published
- 1993-09
- Volume
- 12
- Issue
- 1-3
- Pages
- 179-206
- ISSN
- 0168-6445 (ISSN-L)
- 1574-6976
- OpenAlex
- W2133534556
- Cited by
- 310
- References
- 165
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 7 · 2023: 1 · 2022: 5 · 2021: 5 · 2020: 4 · 2019: 6 · 2018: 8 · 2017: 8 · 2016: 1 · 2015: 5 · 2014: 5 · 2013: 5 · 2012: 15
- FWCI
- 14.52
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEMS Microbiology Reviews (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Keywords
- proteolytic system, lactic acid bacteria, lactococci, protein degradation, cell envelope proteinase, proteolytic enzymes, amino acid transport, peptide transport, nitrogen source, dairy industry
- MeSH terms
- Amino Acid Sequence, Animals, Caseins, Cattle, Cell Membrane, Gram-Positive Bacteria, Lactates, Molecular Sequence Data, Peptide Hydrolases, Lactococcus, Lactic Acid
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