Hostname: page-component-8448b6f56d-dnltx Total loading time: 0 Render date: 2024-04-23T17:26:44.134Z Has data issue: false hasContentIssue false

A novel technique for differentiation of proteins in the development of acid gel structure from control and heat treated milk using confocal scanning laser microscopy

Published online by Cambridge University Press:  12 July 2006

Alix Dubert-Ferrandon
Affiliation:
School of Food Biosciences, The University of Reading, PO Box 226, Whiteknights, Reading, RG6 6AP, UK
Keshaven Niranjan
Affiliation:
School of Food Biosciences, The University of Reading, PO Box 226, Whiteknights, Reading, RG6 6AP, UK
Alistair S Grandison
Affiliation:
School of Food Biosciences, The University of Reading, PO Box 226, Whiteknights, Reading, RG6 6AP, UK

Abstract

The incorporation of caseins and whey proteins into acid gels produced from unheated and heat treated skimmed milk was studied by confocal scanning laser microscopy (CSLM) using fluorescent labelled proteins. Bovine casein micelles were labelled using Alexa Fluor 594, while whey proteins were labelled using Alexa Fluor 488. Samples of the labelled protein solutions were introduced into aliquots of pasteurised skim milk, and skim milk heated to 90 °C for 2 min and 95 °C for 8 min. The milk was acidified at 40 °C to a final pH of 4·4 using 20 g glucono-delta-lactone/l (GDL). The formation of gels was observed with CSLM at two wavelengths (488 nm and 594 nm), and also by visual and rheological methods. In the control milk, as pH decreased distinct casein aggregates appeared, and as further pH reduction occurred, the whey proteins could be seen to coat the casein aggregates. With the heated milks, the gel structure was formed of continuous strands consisting of both casein and whey protein. The formation of the gel network was correlated with an increase in the elastic modulus for all three treatments, in relation to the severity of heat treatment. This model system allows the separate observation of the caseins and whey proteins, and the study of the interactions between the two protein fractions during the formation of the acid gel structure, on a real-time basis. The system could therefore be a valuable tool in the study of structure formation in yoghurt and other dairy protein systems.

Type
Research Article
Copyright
Proprietors of Journal of Dairy Research 2006

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.)