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Enhancement of proteolysis in bovine skim milk by heat and chemical treatments

Published online by Cambridge University Press:  01 June 2009

Yasuo Igarashi
Yasuo Igarashi
Affiliation:
Faculty of Agriculture, Hirosaki University, Hirosaki, Aomori 036, Japan
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Summary

Effect of heating and of some chemical treatments on the proteolysis of skim milk caused by its major proteinase system, plasmin, was investigated. Degree of proteolysis was expressed as the increase in γ-casein content of skim milk (mg/ml) after incubation with 0·02% (w/v) NaN3 at 37 °C for 20 h. Apart from reduced proteolysis in skim milk heated at > 70 °C for 10 min or at 75 °C for ∼ 5 min, some enhancement (10–80%) was observed on heating at 55–63 °C for 10 min or at 60–65 °C for 15 s. Heating at pasteurization conditions (63 °C/30 min or 72 °C/15 s) had no apparent effect on the amount of proteolysis. Addition of ascorbic acid (0·2 mg/100 ml) or H2O2 (1/100 ml) to unheated skim milk also increased the amount of proteolysis by 38 and 28%, respectively. However, the extent of this increase diminished with increasing amounts of both chemicals. Furthermore, there was a steady increase (∼ 33%) in proteolysis with time of exposure to light for up to 3 h. These results suggest that oxidative conditions lead skim milk to enhanced proteolysis by inactivating an inhibitor(s) operating in the plasmin system in milk.

Type
Original Articles
Information
Journal of Dairy Research , Volume 57 , Issue 4 , November 1990 , pp. 541 - 548
Copyright
Copyright © Proprietors of Journal of Dairy Research 1990

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References

REFERENCES

Alichanidis, E., Wrathall, J. H. M. & Andrews, A. T. 1986 Heat stability of plasmin (milk proteinase) and plasminogen. Journal of Dairy Research 53 259–269CrossRefGoogle ScholarPubMed
Allen, J. C. & Joseph, G. 1985 Review article. Deterioration of pasteurized milk on storage. Journal of Dairy Research 52 469–487CrossRefGoogle Scholar
Andrews, A. T. 1983 Proteinases in normal bovine milk and their action on caseins. Journal of Dairy Research 50 45–55CrossRefGoogle ScholarPubMed
Andrews, A. T. & Alichanidis, E. 1983 Proteolysis of caseins and the proteose-peptone fraction of bovine milk. Journal of Dairy Research 50 275–290CrossRefGoogle ScholarPubMed
Björck, L. 1973 Modifications of casein in ultra-high-temperature treated milk during storage. Milchwissenschaft 28 291–293Google Scholar
Corradini, C. 1975 Gel formation behaviour in UHT sterilized milk. Milchwissenschaft 30 413–416Google Scholar
De Rham, O. & Andrews, A. T. 1982 The roles of native milk proteinase and its zymogen during proteolysis in normal bovine milk. Journal of Dairy Research 49 577–585CrossRefGoogle ScholarPubMed
Driessen, F. M. & Van Der Waals, C. B. 1978 Inactivation of native milk proteinase by heat treatment. Netherlands Milk and Dairy Journal 32 245–254Google Scholar
Dulley, J. R. 1972 Bovine milk protease. Journal of Dairy Research 39 1–9CrossRefGoogle ScholarPubMed
Fox, P. F. 1989 Proteolysis during cheese manufacture and ripening. Journal of Dairy Science 72 1379–1400CrossRefGoogle Scholar
Grufferty, M. B. & Fox, P. F. 1988 Review article. Milk alkaline proteinase. Journal of Dairy Research 55 609–630CrossRefGoogle ScholarPubMed
Honkanen-Buzalski, T. & Sandholm, M. 1981 Trypsin-inhibitors in mastitic milk and colostrum: correlation between trypsin-inhibitor capacity, bovine serum albumin and somatic cell contents. Journal of Dairy Research 48 213–223CrossRefGoogle ScholarPubMed
Hsu, H.-Y. & Shipe, W. F. 1986 Effects of some chemical and physical treatments on proteolysis in milk. Journal of Dairy Science 69 1491–1497CrossRefGoogle Scholar
Humbert, G. & Alais, C. 1979 Review of the progress of Dairy Science: The milk proteinase system. Journal of Dairy Research 46 559–571CrossRefGoogle ScholarPubMed
Igarashi, Y. 1989 A method for determination of γ-casein and its use for investigating proteolysis in bovine milk. Journal of Dairy Research 56 619–629CrossRefGoogle Scholar
Igoshi, K., Kaminogawa, S. & Yamauchi, K. 1986 Profiles of proteinases in Gouda-type cheese. Journal of Dairy Science 69 2018–2026CrossRefGoogle Scholar
Kaminogawa, S., Yamauchi, K. & Tsugo, T. 1969 Properties of milk protease concentrated from acid-precipitated casein. Japanese Journal of Zootechnical Science 40 559–565Google Scholar
Kitchen, B. J. 1985 Indigenous milk enzymes. In Developments in Dairy Chemistry – 3. Lactose and Minor Constituents pp. 239–279 (Ed. Fox, P. F.). London: Elsevier Applied Science PublishersGoogle Scholar
Korycka-Dahl, M., Ribadeau, Dumas B., Chene, N. & Martal, J. 1983 Plasmin activity in milk. Journal of Dairy Science 66 704–711CrossRefGoogle Scholar
Korycka-Dahl, M. & Richardson, T. 1978 Photogeneration of Superoxide anion in serum of bovine milk and in model systems containing riboflavin and amino acids. Journal of Dairy Science 61 400–407CrossRefGoogle Scholar
Lawrence, D. A. & Loskutoff, D. J. 1986 Inactivation of plasminogen activator inhibitor by oxidants. Biochemistry 25 6351–6355CrossRefGoogle ScholarPubMed
Noomen, A. 1975 Proteolytic activity of milk protease in raw and pasteurized cow's milk. Netherlands Milk and Dairy Journal 29 153–161Google Scholar
Ollikainen, P. & Kivelä, T. 1989 The importance of plasmin in Swiss-type cheese ripening. Milchwissenschaft 44 204–206Google Scholar
Reimerdes, E. H., Halpaap, I. & Klostermeyer, H. 1981 [Milk proteinases. 10. Enzyme-kinetic comparison of bovine plasmin with two milk proteinases.] Milchwissenschaft 36 73–79Google Scholar
Reimerdes, E. H., Klostermeyer, H. & Sayk, E. 1976 [Milk proteinases. 7. Fractionation of components of the proteinase inhibitor system in milk.] Milchwissenschaft 31 329–334Google Scholar
Richardson, B. C. 1983 The proteinases of bovine milk and the effect of pasteurization on their activity. New Zealand Journal of Dairy Science and Technology 18 233–245Google Scholar
Richardson, B. C. & Pearce, K. N. 1981 The determination of plasmin in dairy products. New Zealand Journal of Dairy Science and Technology 16 209–220Google Scholar
Rollema, H. S., Visser, S. & Poll, J. K. 1981 On the determination, purification and characterization of the alkaline proteinase from bovine milk. Netherlands Milk and Dairy Journal 35 396–399Google Scholar
Rollema, H. S., Visser, S. & Poll, J. K. 1983 Spectrophotometric assay of plasmin and plasminogen in bovine milk. Milchwissenschaft 38 214–217Google Scholar
Searle, A. J. F. & Willson, R. L. 1983 Stimulation of microsomal lipid peroxidation by iron and cysteine. Characterization and the role of free radicals. Biochemical Journal 212 549–554CrossRefGoogle ScholarPubMed
Snoeren, T. H. M., Van Der Speck, C. A., Dekker, R. & Both, P. 1979 Proteolysis during the storage of UHT-sterilized whole milk. 1. Experiments with milk heated by the direct system for 4 seconds at 142 °C. Netherlands Milk and Dairy Journal 33 31–39Google Scholar
Stief, T. W., Lenz, P., Becker, U. & Heinburger, N. 1988 Functional determination of plasminogen activator inhibitor (PAI) based on oxidative inactivation of alpha 2-antiplasmin: no influence of sample heparin and fibrinogen split products (FSP). Fibrinolysis 2 Suppl. 2 73–74Google Scholar
Yee, J. J. & Shipe, W. F. 1982 Effects of sulfhydryl compounds on lipid oxidations catalyzed by copper and heme. Journal of Dairy Science 65 1414–1420CrossRefGoogle Scholar