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Cited by 160Enzyme Production and CharacterizationProbiotics and Fermented FoodsProteins in Food Systems

Comparative Study of Action of Cell Wall Proteinases from Various Strains of Streptococcus cremoris on Bovine α s1 -, β-, and κ-Casein

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Visser, Servaas, Exterkate, Fred A., Slangen, Charles J., de Veer, Gerrie J. C. M.·1986·Applied and Environmental Microbiology
DOI 10.1128/aem.52.5.1162-1166.1986PMC PMC239191
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Abstract

Partially purified cell wall proteinases of eight strains of Streptococcus cremoris were compared in their action on bovine alpha(s1)-, beta-, and kappa-casein, as visualized by starch gel electrophoresis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and thin-layer chromatography. Characteristic degradation profiles could be distinguished, from which the occurrence of two proteinases, represented by strain HP and strain AM(1), was concluded. The action of the HP-type proteinase P(1) (also detectable in strains Wg(2), C(13), and TR) was established by electrophoretic methods to be directed preferentially towards beta-casein. The AM(1)-type proteinase P(III) (also detectable in strain SK(11)) was also able to degrade beta-casein, but at the same time split alpha(s1)- and kappa-casein more extensively than did P(I). Strain FD(27) exhibited mainly P(I) activity but also detectable P(III) degradation characteristics. The cell wall proteinase preparation of strain E(8) showed low P(I) as well as low P(III) activity. All proteinase preparations produced from kappa-casein positively charged degradation products with electrophoretic mobilities similar to those of degradation products released by the action of the milk-clotting enzyme chymosin. The differences between P(I) and P(III) in mode of action, as detected by gel electrophoresis and thin-layer chromatography, were reflected by the courses of the initial degradation of methyl-C-labeled beta-casein and by the effect of alpha(s1)- plus kappa-casein on these degradations. The results are discussed in the light of previous comparative studies of cell wall proteinases in strains of S. cremoris and with respect to the growth of this organism in milk.

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Crossref · 10.1128/aem.52.5.1162-1166.1986

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  • Some PrtP enzymes (PI type) prefer β-casein and all types cleave β-casein at multiple sites with no obvious specificity.

    “Some PrtP enzymes (PI type) prefer β-casein and all types cleave β- casein at multiple sites with no obvious specificity (Visser et al., 1986; Exterkate et al., 1993; Børsting et al., 2015).”

    From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Visser et al., 1986

    The Discussion reports that the HP-type proteinase preferentially acts on β-casein, while the Results show that both HP- and AM1-type activities degrade it. The paper describes characteristic, different degradation patterns for the two types, but does not establish cleavage at multiple sites with no obvious specificity. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • The CEP enzymes are selective regarding which caseins to hydrolyze and they leave whey proteins unhydrolyzed.

    “The CEP enzymes are selective regarding which caseins to hydrolyze and they leave whey proteins unhydrolyzed (Visser et al., 1986).”

    From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Visser et al., 1986

    The Discussion reports that the cell-wall proteinases differ in their action on αs1-, β-, and κ-casein, supporting selectivity among caseins. The paper describes experiments on caseins, but our copy does not establish that whey proteins are left unhydrolyzed. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

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Authors
Visser, S., Exterkate, F. A., Slangen, C. J., & de Veer, G. J. C. M.
Affiliations
Netherlands Institute for Dairy Research, 6710 BA Ede, The Netherlands
Venue
Applied and Environmental Microbiology
Publisher
American Society for Microbiology
Published
1986-11
Volume
52
Issue
5
Pages
1162-1166
ISSN
  • 0099-2240 (ISSN-L)
  • 1098-5336
DOI
10.1128/aem.52.5.1162-1166.1986
PMC
PMC239191
OpenAlex
W291911162
Cited by
160
References
14
Citations by year
2026: 2 · 2025: 2 · 2024: 1 · 2023: 3 · 2022: 1 · 2021: 1 · 2020: 3 · 2018: 1 · 2017: 3 · 2015: 1 · 2014: 4 · 2013: 1 · 2012: 3
FWCI
9.77
Type
journal article
Language
en
Open access
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
Locations
  • Applied and Environmental Microbiology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
Keywords
Streptococcus cremoris, bovine casein, αs1-casein, β-casein, kappa-casein, casein degradation, chymosin, milk-clotting enzyme, strain differences, milk

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