Hostname: page-component-586b7cd67f-rcrh6 Total loading time: 0 Render date: 2024-12-02T19:32:01.657Z Has data issue: false hasContentIssue false

The release of peptides and glycopeptides by the action of heat on cow's milk

Published online by Cambridge University Press:  01 June 2009

E. J. Hindle
Affiliation:
School of Biological Sciences, The University, Bradford 7
J. V. Wheelock
Affiliation:
School of Biological Sciences, The University, Bradford 7

Summary

The release, as a result of heat treatment on cow's milk, of peptides and glycopeptides which are soluble in the 12% trichloroacetic acid (TCA) filtrate of the milk has been studied. The results showed that the amount of peptides released increased with temperature and duration of the heat treatment. There were differences between milks in their response to a given heat treatment. Glycopeptides were released at temperatures as low as 50 °C but not at 37 °C. A comparison was made of the glycopeptides released by heat treatment and of those released from κ-casein by the action of rennin on the milk. This showed that N-acetyl neuraminic acid, D-galactose and 2-acetamido-2-deoxy-D-galactose were invariably present in both groups of glycopeptides. D-Mannose was also present in the glycopeptides released by heat but was detected on the glycopeptides released by rennin in only one of 6 experiments. It is suggested that glycopeptides released by heat may be derived from κ-casein but that a definite conclusion cannot be reached at present because of lack of information on the carbohydrates attached to other milk proteins.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1970

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

Alais, C. & Jollès, P. (1961). Biochim. biophys. Acta 51, 315.CrossRefGoogle Scholar
Alais, C., Kiger, N. & Jollès, P. (1967). J. Dairy Sci. 50, 1738.CrossRefGoogle Scholar
Armstrong, C. E., Mackinlay, A. G., Hill, R. J. & Wake, R. G. (1967). Biochim. biophys. Acta 140, 123.CrossRefGoogle Scholar
Burton, H. (1969). Dairy Sci. Abstr. 31, 287.Google Scholar
Clamp, J. R., Dawson, G. & Hough, L. (1967). Biochim. biophys. Acta 148, 342.CrossRefGoogle Scholar
Dawson, G. & Clamp, J. R. (1968). Biochem. J. 107, 341.CrossRefGoogle Scholar
De Koning, P. J., Jenness, R. & Wijnand, H. P. (1963). Ned. Melk- en Zuiveltijdschr. 17, 352.Google Scholar
Howat, G. R. & Wright, N. C. (1934). Biochem. J. 28, 1336.CrossRefGoogle Scholar
Jollès, P., Alais, C., Adam, A., Delfour, A. & Jollès, J. (1964). Chimia 18, 357.Google Scholar
Kuwata, J., Niki, R. & Arima, S. (1969). J. agric. chem. Soc. Japan 43, 183.Google Scholar
McCabe, E. M. (1967). Ph.D. Thesis, Michigan State University.Google Scholar
McKenzie, H. A. (1967). Adv. Protein Chem. 22, 55.CrossRefGoogle Scholar
Reynolds, L. M., Henneberry, G. O. & Baker, B. E. (1959). J. Dairy Sci. 42, 1463.CrossRefGoogle Scholar
Rothfus, J. A. & Smith, E. L. (1963). J. biol. Chem. 238, 1402.CrossRefGoogle Scholar
Schmidt, D. G. (1968). Ned. Melk- en Zuiveltijdschr. 22, 40.Google Scholar
Sinkinson, G. & Wheelock, J. V. (1970 a). J. Dairy Res. 37, 113.CrossRefGoogle Scholar
Sinkinson, G. & Wheelock, J. V. (1970 b). Biochim. biophys. Acta (in the press).Google Scholar
Spragg, B. P. & Clamp, J. R. (1969). Biochem. J. 114, 57.CrossRefGoogle Scholar
Wheelock, J. V. & Sinkinson, G. (1969). Biochim. biophys. Acta 194, 597.CrossRefGoogle Scholar
Yaguchi, M., Davies, D. T. & Kim, Y. K. (1968). J. Dairy Sci. 51, 473.CrossRefGoogle Scholar
Yoshino, U., Samuro, M., Yamauchi, K. & Tsugo, T. (1964). Agric. biol. Chem. 28, 82.CrossRefGoogle Scholar