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Influence of processing on the molecular modifications of milk proteins in the course of enzymic coagulation

Published online by Cambridge University Press:  01 June 2009

Stefania Iametti ,
Roberto Giangiacomo ,
Giorgio Messina  and
Francesco Bonomi
Stefania Iametti
Affiliation:
Dipartimento di Scienze Molecolari Agroalimentari, Sezione di Biochimica, Università di Milano, Italia
Roberto Giangiacomo
Affiliation:
Istituto Lattiero-Caseario, Ministero dell' Agricoltura e Foreste, Sezione di Tecnologie Applicative, Lodi, Italia
Giorgio Messina
Affiliation:
Istituto Lattiero-Caseario, Ministero dell' Agricoltura e Foreste, Sezione di Tecnologie Applicative, Lodi, Italia
Francesco Bonomi
Affiliation:
Dipartimento di Scienze Molecolari Agroalimentari, Sezione di Biochimica, Università di Milano, Italia
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Summary

The formation of hydrophobic sites on the surface of casein micelles as a consequence of enzymic coagulation of industrially heat-treated milk was studied by following the distribution of a fluorescent hydrophobic probe between a free and an aggregated protein fraction. Results were compared with those obtained when coagulation of the same milk samples was followed rheologically in a Gelograph apparatus and by tristimulus colorimetry. Thermal treatment of milk appeared to affect the accessibility of casein to enzyme action, while homogenization influenced the rate of cooperative aggregation of casein subjected to proteolysis.

Type
Original Articles
Information
Journal of Dairy Research , Volume 60 , Issue 2 , May 1993 , pp. 151 - 159
Copyright
Copyright © Proprietors of Journal of Dairy Research 1993

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References

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