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The action of rennet on whole milk

Published online by Cambridge University Press:  01 June 2009

J. V. Wheelock
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading
Dorothy J. Knight
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading

Summary

The release, by the action of rennet, of peptides which are soluble in trichloroacetic acid (TCA) has been studied using milk samples from individual cows. This release showed an initial marked increase with time of rennet action. After the milk clotted there was no further increase for at least 30 min. There was considerable variation in the total amount of N and of sialic acid released from milk samples taken from individual animals at different times during the lactation.

For a given milk sample treated with rennet, the amount of sialic acid in the filtrate obtained after precipitation with 2% TCA was similar to that obtained with 10% TCA, whereas the amount of nitrogen was much greater with the 2 % TCA. It appeared that the peptides containing sialic acid were released at a slower rate.

On average, about half the total sialic acid in the casein was recovered in the TCA filtrate after rennet action, which suggests that either a proportion of the κ-casein was not accessible to enzyme action or the technique used did not permit full recovery of the sialic acid-containing peptides.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1969

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References

REFERENCES

Alais, C. (1963). Annls Biol. anim. Biochim. Biophys. 3, 391.CrossRefGoogle Scholar
Alais, C., Blondel-Quéroix, J. S. & Jollès, P. (1964). Bull. Soc. Chim. biol. 46, 973.Google Scholar
Alais, C., Mocquot, G., Nitschmann, H. & Zahler, P. (1953). Helv. chim. Acta 36, 1955.CrossRefGoogle Scholar
Aschaffenburg, R. & Drewry, J. (1959). 15th Int. Dairy. Congr., London 3, 1631.Google Scholar
Beeby, R. (1963). J. Dairy Res. 30, 77.CrossRefGoogle Scholar
Berridge, N. J. (1954). Adv. Enzymol. 15, 423.Google Scholar
Cerbulis, J., Custer, J. H. & Zittle, C. A. (1959). Archs Biochem. Biophys. 84, 417.CrossRefGoogle Scholar
Cheeseman, G. C. (1966). In Methods for the Determination of Amino Acid Composition of Milk Proteins, p. 50 (ed. Brunfeldt, K.). Copenhagen: Danish Institute of Protein Chemistry.Google Scholar
Chen, Shi-Han & Sutton, H. E. (1967). Genetics 56, 425.CrossRefGoogle Scholar
Foltmann, B. (1959). 15th Int. Dairy Congr., London 2, 655.Google Scholar
Gibbons, R. A. & Cheeseman, G. C. (1962). Biochim. biophys. Acta 56, 354.CrossRefGoogle Scholar
Haberman, W., Mattenheimer, H., Sky-Peck, H. & Singhara, H. (1961). Chimia 15, 339.Google Scholar
Kim, Y. K., Arima, S. & Yasui, T. (1967). Jap. J. zootech. Sci. 38, 62.Google Scholar
MacKinlay, A. G. & Wake, R. G. (1965). Biochim. biophys. Acta 104, 167.CrossRefGoogle Scholar
Malpress, F. H. & Hytten, F. E. (1964). Biochem. J. 91, 130.CrossRefGoogle Scholar
Marier, J. R., Tessier, H. & Rose, D. (1963). J. Dairy Sci. 46, 764.CrossRefGoogle Scholar
Nitschmann, H. & Bohren, H. U. (1955). Helv. chim. Acta 38, 1953.CrossRefGoogle Scholar
Nitschmann, H. & Keller, W. (1955), Helv. chim. Acta 38, 942.CrossRefGoogle Scholar
Nitschmann, H., Wissman, H. & Henzi, R. (1957). Chimia 11, 76.Google Scholar
Verpoorte, J. A., Green, W. A. & Kay, C. M. (1965). J. biol. Chem. 240, 1156.CrossRefGoogle Scholar
Warren, L. (1959). J. biol. Chem. 234, 1971.CrossRefGoogle Scholar
Waugh, D. F. & Von Hippel, P. H. (1956). J. Am. chem. Soc. 78, 4576.CrossRefGoogle Scholar