CoChat
Sign Up
Cited by 305Probiotics and Fermented FoodsEnzyme Production and CharacterizationProteins in Food Systems

Proteolytic Enzymes and Their Relation to Cheese Ripening and Flavor: An Overview

Open access
Visser, Servaas·1993·Journal of Dairy Science
DOI 10.3168/jds.s0022-0302(93)77354-3
Open this paper in CoChat — free account

Abstract

Proteolytic events taking place during cheese ripening are described, and the characteristics of the various proteolytic systems involved are reviewed.Some emphasis is placed on the proteolytic enzymes from starter bacteria because these, in particular, have been subjects of recent and current research.In cheese, the concerted action of residual milk-clotting enzyme, indigenous milk proteinases, and starter proteinases provides suitable substrates for the starter peptidases, which ultimately generate small peptides and free amino acids.Deviations from such a delicately balanced process may lead to deviations from the desired cheese texture and flavor.A bitter flavor defect may develop in the ripening cheese when the degradation of slowly accumulating bitter peptides by suitable peptidases is inhibited.Cheese flavor is thought to be mainly generated by the further, nonproteolytic conversion of amino acids via enzymic and nonenzymic reactions.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3168/jds.s0022-0302(93)77354-3

Cites

177 of 177 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

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?

  • Most plant-derived clotting enzymes have high proteolytic activity, causing bitter compounds in cheese.

    “The high PA characterizes most of the vegetable proteases, which, especially during beginning of cheeses ripening, continue to hydrolyze the caseins causing the appearance of short peptides, which can have a bitter taste [80].”

    From Plant Milk-Clotting Enzymes for Cheesemaking (2022) · cites this paper as [80]

    The Introduction (page unavailable) says residual clotting enzyme contributes to casein breakdown during initial ripening, and the ‘Bitter Flavor Formation and Debittering’ section (page unavailable) links bitter peptides to residual clotting enzyme and bacterial proteinases. The passages do not establish that most plant-derived clotting enzymes have high proteolytic activity or specifically cause this effect. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • In long-ripened cheeses, the autolysis of SLAB can provide sufficient nutrients to support the growth of non-starter LAB (NSLAB) in vitro.

    “In long-ripened cheeses, it has also been observed that the autolysis of SLAB can provide sufficient nutrients to support the growth of non-starter LAB (NSLAB) in vitro [18,53,73,77,93,99,100,101,102].”

    From Microbiota of Cheese Ecosystems: A Perspective on Cheesemaking (2025) · cites this paper as [101]

    The introductory overview (page unavailable) says that proteolytic enzymes from nonstarter bacteria are not considered. The discussion of starter-cell lysis (page unavailable) addresses whether cell contents escape into cheese, but does not say that autolysis supplies sufficient nutrients for NSLAB growth in vitro. Searches for nonstarter bacteria, nutrients and in-vitro growth found no passage establishing that claim. (LLM, conf=0.77)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

18 of the 195 references couldn’t be matched to a known paper.

Research works printed but not linked: 13

  1. de Koning, P. J., G. van den Berg, and E. de Vries. 1981. Milk clotting enzymes. 2. Use of rennet substi- tutes. Voedingsmiddelentechnologie 14(11):27.
  2. P. F. Fox, ed. Elsevier Appl. Sci., London, Eng!.
  3. P. F. Fox. ed. Elsevier Appl. Sci., London, Engl.
  4. Grufferty, M. B.• and P. F. Fox. 1983. The action of plasmin on asl-casein. Page 24 in Research in Food Science and Nutrition. Vol 2. J. V. McLoughlin and B. M. McKenna. ed. Boole Press. Dublin, Ireland.
  5. Haandrikman. A. 1., I. Kok. H. Laan, S. Soemitro, A. Journal of Dairy Science Vol. 76, No. I, 1993
  6. Humbert, G., and C. Alais. 1979. Review of the progress of dairy science: the milk proteinase system. J. Dairy Res. 46:559.
  7. International Dairy Federation. 1991. Monograph on chemical methods for evaluating proteolysis in cheese maturation. IDF Bull. 261. Int. Dairy Fed., Brussels, Belgium. 87 International Union of Biochemistry. 1984. Recom- mendations of the nomenclature committee of the IUB. Academic Press, Inc., London, Engl.
  8. III Law, B. A. 1987. Proteolysis in relation to nonna! and accelerated cheese ripening. Page 365 in Cheese: Chemistry, Physics and Microbiology. Vol. 1. P. F. Fox, ed. Elsevier Appl. Sci., London, Engl. 112
  9. Manning, D. J. 1978. The chemical basis of Cheddar flavor. Dairy Ind. lnt. 43(4):37. 119
  10. 1450hmiya, K., and Y. Sato. 1975. Purification and Journal of Dairy Science Vol. 76, No. I, 1993 propenies of intracellular proteinase from Strep- tococcus cremoris. Appl. Microbiol. 30:738. 146
  11. Stadhouders, 1. 1978. Mechanism of the formation of the bitter flavour defect in cheese. Section 39 ST in Proc. XX Int. Dairy Congr., Paris, France. Int. Dairy Fed., Brussels, Belgium. 172 Stadhouders, 1., and G. Hup. 1975. Factors affecting bitter flavour in Gouda cheese. Neth. Milk Dairy 1. 29:335. 173 Stadhouders, 1., G. Hup, F. A. Exterkate, and S. Visser. 1983. Bitter flavour in cheese. 1. Mechanism of the formation of the bitter flavour defect in cheese. Neth. Milk Dairy J. 37:157. 174
  12. P. F. Fox, ed. Elsevier Appl. Sci., London, Engl. 175
  13. Visser, S. 1981. Proteolytic enzymes and their action on milk proteins. A review. Neth. Milk Dairy 1. 35: 65. 194

Cited by

Sorted by citations

Related

Authors
Visser, S.
Affiliations
Nederlands Instituut Voor Zuivel Oonderzoek (NL)
Corresponding author
Visser, Servaas
Venue
Journal of Dairy Science
Publisher
American Dairy Science Association
Published
1993-01
Volume
76
Issue
1
Pages
329-350
ISSN
0022-0302 (ISSN-L)
DOI
10.3168/jds.s0022-0302(93)77354-3
OpenAlex
W2027602106
Cited by
305
References
195
Citations by year
2026: 4 · 2025: 1 · 2024: 4 · 2023: 6 · 2022: 7 · 2021: 6 · 2020: 2 · 2019: 4 · 2018: 8 · 2017: 10 · 2016: 7 · 2015: 2 · 2014: 13 · 2013: 5 · 2012: 5
FWCI
34.48
Type
journal article
Language
en
Open access
Licence
Locations
Journal of Dairy Science (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 › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
Keywords
proteolytic enzymes, cheese ripening, cheese flavor, starter bacteria, milk-clotting enzyme, bitter peptides, cheese texture, amino acid conversion, free amino acids

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