Author:
Iametti Stefania,Giangiacomo Roberto,Messina Giorgio,Bonomi Francesco
Abstract
SummaryThe 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.
Publisher
Cambridge University Press (CUP)
Subject
Animal Science and Zoology,General Medicine,Food Science
Reference25 articles.
1. Real-time monitoring of the surface hydrophobicity changes associated with isothermal treatment of milk and milk protein fractions;Bonomi;Milchwissenschaft,1991
2. A study of surface hydrophobicity of milk proteins during enzymic coagulation and curd hardening
3. The effect of heat treatment on the colour of milk. II. Practical applications of colour measurement in the control of heat treatment;Burton;Dairy Industries,1956
4. Effect of storage, light and homogenization on the colour of ultra heat treated and sterilized milk
Cited by
8 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献