CoChat
Sign Up
Cited by 593Proteins in Food SystemsMilk Quality and Mastitis in Dairy CowsAdvanced Scientific Research Methods

The DOI matches its Crossref record; 178 of the 189 references it cites were found in a registry or an index.

Proteolysis During Cheese Manufacture and Ripening

Open access
Fox, P.F.·1989·Journal of Dairy Science
DOI 10.3168/jds.s0022-0302(89)79246-8
Open this paper in CoChat — free account

Abstract

Proteolysis in cheese can be divided into three phases: proteolysis in milk before cheese manufacture, the enzymatically induced coagulation of the milk, and proteolysis during cheese ripening.Extracellular proteinases from psychrotrophs may cause reduced cheese yields and off-flavors, but the problem does not appear to be significant at populations <106 cfu/ml.Proteinases from leucocytes may also reduce yields, but these are less active than bacterial proteinases.Plasmin (indigenous milk proteinase)causes significant hydrolysis of [$-casein, especially in late lactation, but because most of this occurs prior to milking, yield losses due to plasmin activity (i.e., via formation of proteose peptones) are largely unavoidable.Coagulation of milk for rennet cheeses is accomplished by the specific cleavage of the casein miceUe-stabilizing protein, g-casein, at the phenylalanine (105)methionine (106) bond by acid proteinases (rennets).The significance of the primary, secondary, and tertiary structures of g-casein on the sensitivity of this bond is now established, as are pH, ionic strength, temperature, heat treatment of milk, and environmental and processing variables.Proteolysis is probably the most important biochemical event during the ripening of most cheese varieties, with a major impact on flavor and texture.Tech-

Overview

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(89)79246-8

Cites

178 of 178 references verified0 citation errors · 0 not checkable

Statistics

Verification

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?

Self-check

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

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

Citations

Cites

Show all 189 references

Research works printed but not linked: 56

  1. Aston, 1986, Contribution of the components of the water-soluble fraction to the flavour of Cheddar cheese, N. Z. J. Dairy Sci. Technol., 21, 229
  2. Aston, 1983, Proteolysis and flavour development in Cheddar cheeses subjected to accelerated ripening treatments, Aust. J. Dairy Technol., 38, 59
  3. Banks, 1985, Incorporation of the protein from starter growth medium in cheese curd during manufacture of Cheddar cheese, Milchwissenschaft, 40, 209
  4. Bican, 1982, Milk protein analysis, a high performance chromatography study, Milchwissenschaft, 37, 592
  5. Castberg, 1976, Degradation of milk proteins by enzymes from lactic acid bacteria used in cheese making A review, Milchwissenschaft, 31, 85
  6. Creamer, 1974, Identification of the primary degradation product of αS1-casein in Cheddar cheese, N. Z. J. Dairy Sci. Technol., 9, 9
  7. de Jong, 1975, A quantitative electrophoretic method of studying cheese ripening, Neth. Milk Dairy J., 29, 162
  8. de Koning, 1978, Applications of a synthetic hexapeptide as a standard substrate for the determination of the activity of chymosin, Neth. Milk Dairy J., 32, 232
  9. Desmazeaud, 1977, General mechanism of protein breakdown during cheese ripening, Milchwissenschaft, 32, 731
  10. Donnelly, 1984, Casein micelle composition and syneresis properties of late lactation milk, Ir. J. Food Sci. Technol., 8, 121
  11. Ernstrom, C. A. Milk clotting enzymes. Pages 662–771 w Fundamentals of dairy chemistry. 2nd ed.In: B. H. Webb, A. H. Johnson, and J. A. Alford, (Eds.), AVI Publ. Co., Inc., Westport, CT.
  12. Fedrick, 1986, The effects of increased starter populations, added neutral proteinase and elevated temperature storage on Cheddar cheese manufacture and maturation, N. Z. J. Dairy Sci. Technol., 21, 191
  13. Fiat, 1977, Donnees structurales concemant le caseinoglycopeptide humain et comparisons avec les caseinoglycopeptides de rummants, C. R. Acad. Sci. Paris, Ser. D., 284, 393
  14. Foltmann, 1981, Mammalian milk-clotting proteases: structure, function, evolution and development, Neth. Milk. Dairy J., 35, 223
  15. Fox, 1981, Proteinases in dairy technology, Neth. Milk Dairy J., 35, 233
  16. Fox, 1987, Vol. 1 and 2
  17. Grieve, 1983, Use of Streptococcus lactis lac mutants for accelerating cheese ripening. 2. Their effect on the rate of proteolysis and flavour development, Aust. J. Dairy Technol., 38, 49
  18. Gripon, 1987, Mould-ripened cheeses, Vol.2, 121
  19. Grufferty, 1988, Functional properties of casein hydrolyzed by alkaline milk proteinase, N.Z. J. Dairy Sci. Technol., 23, 95
  20. Grufferty, 1988, Factors affecting the release of alkaline milk proteinase from casein micelles, N.Z J. Dairy Sci. Technol., 23, 153
  21. Hickey, 1983, Amino acid accumulation in Cheddar cheese manufactured from normal and ultrafiltered milk, Aust. J. Dairy Technol., 38, 110
  22. Hill, 1978, A study of the structural factors that affect the reactivity of the chymo-sin-sensitive bond in κ-casein, N. Z. J. Dairy Sci. Technol., 13, 195
  23. Huber, 1974, Isolierung und Identifizierung eines Bitterstoffes aus Butterkase, Milchwissenschaft, 29, 449
  24. Humme, 1972, The optimum pH for the limited specific proteolysis of κ-casein by rennin (primary phase of milk clotting), Neth. Milk Dairy J., 26, 180
  25. Humphrey, 1984, High performance ion-exchange cbromatography of the major bovine milk proteins, N. Z J. Dairy Sci. Technol., 19, 197
  26. Ismail, 1972, Accumulation of free amino acids during cheese ripening of some types of Danish cheese, Milchwissenschaft, 27, 556
  27. Jarrett, 1982, A simple method for estimating free amino acids in Cheddar cheese, Aust. J. Dairy Technol., 37, 55
  28. Kaminogawa, 1985, Proteases of lactic acid bacteria in relation to cheese ripening, Jpn. J. Dairy Food Sci., 34, A183
  29. Kleter, 1975, Apparatus for making cheese under strict aseptic conditions, Neth. Milk Dairy J., 29, 295
  30. Kleter, 1974, Aseptic milking of cows, Neth. Milk Dairy J., 28, 212
  31. Kuchroo, 1982, Fractionation of water- soluble nitrogen from Cheddar cheese: chemical methods, Milchwissenschaft, 37, 651
  32. Kuchroo, 1983, Fractionation of the water soluble nitrogen from Cheddar cheese: chromatographic methods, Milchwissenschaft, 38, 76
  33. Kuchroo, 1983, Assessment of proteolysis in cheese by reaction with trinitrobenzene sulphonic acid, Ir. J. Food Sci. Technol., 7, 129
  34. Law, 1984, Microorganisms and their enzymes in the maturation of cheeses, Prog. Ind. Microbiol., 14, 245
  35. Lindqvist, 1963, Investigation of a 37 year old cheese, Milchwissenschaft, 18, 12
  36. Martley, 1972, Cheddar cheese flavour. II. Characteristics of single strain starters associated with good and poor flavour development, N. Z. J. Dairy Sci. Technol., 16, 38
  37. Mathesson, 1981, The immunological determination of chymosin activity in cheese, N. Z. J. Dairy Sci. Technol., 16, 33
  38. Monet, 1986, Specificity of a cell wall proteinase from Streptococcus lactis NCDO 763 toward bovine β-casein, Fed. Eur. Microbiol. Soc. Microbiol. Lett., 36, 127
  39. Ney, 1985, N-Endstandige Aminosauren der Peptide aus reifem Cheddarkase, Milchwissenschaft, 40, 207
  40. Noomen, 1978, Activity of proteolytic enzymes in simulated soft cheese (Meshanger type). 1. Activity of milk protease, Neth. Milk Dairy J., 32, 26
  41. O’Keeffe, 1976, Manufacture of Cheddar cheese under controlled bacteriological conditions, Ir. J. Agric. Res., 15, 151
  42. Payens, 1981, What determines the specificity of chymosin towards κ-casein?, Neth. Milk Dairy J., 35, 387
  43. Phelan, J. A. 1986. Milk coagulants: an evaluation of alternatives to standard calf rennet Ph.D. Thesis, Natl. Univ. Ireland, Dublin.
  44. Reville, 1978, Soluble protein in Cheddar cheese: a comparison of analytical methods, Ir. J. Food Sci. Technol., 2, 67
  45. Richardson, 1984, Plasmin activity in commercial casein and caseinates, N. Z. J. Dairy Sci. Technol., 19, 63
  46. Santoro, 1987, Fractionation of soluble nitrogen in Provolone cheese I, Milchwissenschaft, 42, 709
  47. Schattenkerk, 1973, Relation between structure and capacity to function as a rennin substrate, Neth. Milk Dairy J., 27, 286
  48. Singh, 1972, Changes in peptides and amino acids in cheese during ripening, Milchwissenschaft, 27, 412
  49. Sweeney, K. 1984. Emmental cheese: rheological and chemical changes during ripening. M.Sc. thesis, Natl. Univ. Ireland.
  50. Tokita, 1968, An investigation about Limburger cheese ripening by gel filtration on Sephadex, Milchwissenschaft, 23, 758
  51. Turner, 1986, A microbiological specification for milk for aseptic cheesemaking, N. Z. J. Dairy Sci. Technol., 21, 249
  52. Umemoto, 1978, Direct observation of fine structures of bacteria in ripened Cheddar cheese, Agric. Biol. Chem., 42, 227
  53. Val Hooydonk, 1982, A rapid sensitive high performance liquid chromatography method of following the action of chymosin in milk, Neth. Milk Dairy J., 36, 153
  54. Visser, 1977, Contribution of enzymes from rennet, starter bacteria and milk to proteolysis and flavour development in Gouda cheese. 1. Description of cheese and aseptic cheese-making techniques, Neth. Milk Dairy J., 31, 120
  55. Visser, 1977, Contribution of enzymes from rennet, starter bacteria and milk to proteolysis and flavour development in Gouda cheese. 4. Protein breakdown: a gel electrophoretical study, Neth. Milk Dairy J., 31, 247
  56. Visser, 1983, Bitter flavour in cheese. 3. Comparative gel- chromatographic analysis of hydrophobic peptide fractions from twelve Gouda-type cheese and identification of bitter peptides isolated from a cheese made with Streptococcus cremoris strain HP, Neth. Milk Dairy J., 37, 181

Cited by

Sorted by citations

Items 501–585 of 585

Related

See all

Metadata

Authors
Fox, P. F.
Affiliations
University College Cork (IE)
Corresponding author
Fox, P.F.
Venue
Journal of Dairy Science
Publisher
American Dairy Science Association
Published
1989-06
Volume
72
Issue
6
Pages
1379-1400
ISSN
0022-0302 (ISSN-L)
DOI
10.3168/jds.s0022-0302(89)79246-8
OpenAlex
W2088615413
Cited by
593
References
189
Citations by year
2026: 2 · 2025: 16 · 2024: 12 · 2023: 20 · 2022: 9 · 2021: 12 · 2020: 13 · 2019: 12 · 2018: 18 · 2017: 24 · 2016: 15 · 2015: 18 · 2014: 18 · 2013: 15 · 2012: 12
FWCI
27.39
Type
journal article
Language
en
Open access
Licence
Locations
Journal of Dairy Science (publishedVersion)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Milk Quality and Mastitis in Dairy Cows
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Advanced Scientific Research Methods
Keywords
cheese proteolysis, cheese ripening, milk coagulation, rennet, plasmin, casein, off-flavor, cheese yield, proteose peptone

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