Altered Specificity of Lactococcal Proteinase P I (Lactocepin I) in Humectant Systems Reflecting the Water Activity and Salt Content of Cheddar Cheese
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By using various humectant systems, the specificity of hydrolysis of α s1 -, β-, and κ-caseins by the cell envelope-associated proteinase (lactocepin; EC 3.4.21.96 ) with type P 1 specificity (i.e., lactocepin I) from Lactococcus lactis subsp. lactis BN1 was investigated at water activities (a w ) and salt concentrations reflecting those in cheddar type cheese. In the presence of polyethylene glycol 20000 (PEG 20000)-NaCl (a w = 0.95), hydrolysis of β-casein resulted in production of the peptides comprising residues 1 to 6 and 47 to 52, which are characteristic of type P III enzyme activity (lactocepin III) in buffer. The fragment comprising residues 1 through 166, inclusive (fragment 1-166), which is typical of lactocepin I activity in buffer systems, was not produced. Similarly, peptide 152-160 from κ-casein, which is usually produced in aqueous buffers exclusively by lactocepin III, was a major product of lactocepin I. Most of the specificity differences obtained in the presence of PEG 20000-NaCl were also obtained in the presence of PEG 20000 alone (a w = 0.99). In addition, α s1 -casein, which normally is resistant to lactocepin I activity, was rapidly hydrolyzed in the presence of PEG 20000 alone. Hydrolysis of casein in the presence of PEG 300-NaCl or glycerol-NaCl (both having an a w of 0.95) was generally as expected for lactocepin I activity except that β-casein peptide 47-52 and κ-casein fragment 1-160 were produced; both of these are normally formed by lactocepin III in buffer. The differences in lactocepin specificity obtained in the humectant systems can be attributed to a combination of a w and humectant hydrophobicity, both of which are parameters that are potentially relevant to the cheese-ripening environment.
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Concerning L. lactis, three surface proteins are attributed to the CWAP group: the chromosomally-encoded sex factor CluA, the plasmid-encoded proteinase NisP, and the plasmid-encoded cell serine proteinase PrtP.
“Concerning L. lactis, three surface proteins were attributed to the same group of CWAP: i) the chromosomally-encoded sex factor CluA [22], ii) the plasmid-encoded proteinase NisP [23], and iii) the plasmid-encoded cell serine proteinase PrtP (also called lactocepin [24], which initiates proteolytic degradation of milk casein [25]).”
From Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci (2007) · cites this paper as [24]
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Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci
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- Authors
- Reid, J. R., & Coolbear, T.
- Affiliations
- <!--label omitted: 1-->New Zealand Dairy Research Institute, Palmerston North, New Zealand
- Venue
- Applied and Environmental Microbiology
- Publisher
- American Society for Microbiology
- Published
- 1998-02
- Volume
- 64
- Issue
- 2
- Pages
- 588-593
- ISSN
- 0099-2240 (ISSN-L)
- 1098-5336
- PMC
- PMC106087
- OpenAlex
- W2118895187
- Cited by
- 20
- References
- 29
- Citations by year
- 2021: 1 · 2017: 1 · 2014: 1 · 2012: 2
- FWCI
- 0.58
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Applied and Environmental Microbiology (publishedVersion)
- PubMed Central (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- 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
- Lactococcus lactis subsp. lactis, casein hydrolysis, αs1-casein, β-casein, kappa-casein, polyethylene glycol, humectants, water activity, salt concentration, cheese ripening, cheese proteolysis
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