Hostname: page-component-78c5997874-4rdpn Total loading time: 0 Render date: 2024-11-20T04:52:09.863Z Has data issue: false hasContentIssue false

A study of the heat stabilities of a number of indigenous milk enzymes

Published online by Cambridge University Press:  01 June 2009

Anthony T. Andrews
Affiliation:
AFRC Institute of Food Research, Reading Laboratory (University of Reading), Shinfield, Reading RG2 9AT, UK
Malcolm Anderson
Affiliation:
AFRC Institute of Food Research, Reading Laboratory (University of Reading), Shinfield, Reading RG2 9AT, UK
Peter W. Goodenough
Affiliation:
AFRC Institute of Food Research, Reading Laboratory (University of Reading), Shinfield, Reading RG2 9AT, UK

Summary

Heat stability profiles of a number of indigenous bovine milk enzymes were examined with the object of being able to monitor heat treatments slightly more severe than typical pasteurization conditions by measurements of residual enzyme activity after heating. Assay procedures were limited to simple fluorimetric, or preferably colorimetric, methods that would be most likely to form the basis of a quick, simple and inexpensive test. Both lipoprotein lipase and α-fucosidase were relatively sensitive to heat and were totally inactivated at temperature/time combinations below those of pasteurization, but the latter may be satisfactory for studying temperatures in the range 55–65°C. Rather more heat stable were N-acetyl-β-glucosaminidase and γ-glutamyl transpeptidase, which may be most appropriate for 65–75°C and 70–80°C respectively. Higher temperature treatments between 80 and 90°C could best be investigated by following α-mannosidase or xanthine oxidase activity.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1987

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Alichandis, E., Wrathall, J. H. M. & Andrews, A. T. 1986 Heat stability of plasmin (milk proteinase) and plasminogen. Journal of Dairy Research 53 259269Google Scholar
Anderson, M. 1981 Inhibition of lipolysis in bovine milk by proteose peptone. Journal of Dairy Research 48 247252CrossRefGoogle ScholarPubMed
Andrews, A. T. 1974 Bovine milk acid phosphatase. II. Binding to casein substrates and heat-inactivation studies. Journal of Dairy Research 41 229237CrossRefGoogle ScholarPubMed
Baumrucker, C. R. 1979 γ-Glutamyl transpeptidase of bovine milk membranes: distribution and characterization. Journal of Dairy Science 62 253258Google Scholar
Cerbulis, J. & Farrell, H. M. 1977 Xanthine oxidase activity in dairy products. Journal of Dairy Science 60 170176CrossRefGoogle Scholar
Huang, C. M. & Keenan, T. W. 1972 Preparation and properties of 5′-nucleotidases from bovine milk fat globule membranes. Biochimica et Biophysica Acta 274 246257CrossRefGoogle ScholarPubMed
Kitto, G. B. 1969 Intra- and extramitochondrial malate dehydrogenases from chicken and tuna heart. Methods in Enzymology 13 106116CrossRefGoogle Scholar
Kjellberg, B. & Karlsson, B. W. 1967 Comparative analyses of lactic and malic dehydrogenases and their multiple molecular forms in milk from various animal species and man. Comparative Biochemistry and Physiology 22 397413Google Scholar
Nilsson-Ehle, P. & Schotz, M. C. 1976 A stable, radioactive substrate emulsion for assay of lipoprotein lipase. Journal of Lipid Research 17 536541CrossRefGoogle ScholarPubMed
Owen, A. J. & Andrews, A. T. 1984 A procedure for the complete clarification of milk of various species and its suitability for use with colorimetric measurements. Journal of Dairy Research 51 307315Google Scholar
Reeves, W. J. & Fimognari, G. M. 1966 L-lactic dehydrogenase: heart (H4). Methods in Enzymology 9 288294Google Scholar