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The rebodying of stirred yoghurt: interactions between proteins

Published online by Cambridge University Press:  14 July 2008

Marie Renan
Affiliation:
Inra-Agrocampus Rennes, UMR1253, Science et Technologie du Lait et de l'Œuf, 65 rue de St Brieuc, F-35 042 Rennes cedex, France
Fanny Guyomarc'h
Affiliation:
Inra-Agrocampus Rennes, UMR1253, Science et Technologie du Lait et de l'Œuf, 65 rue de St Brieuc, F-35 042 Rennes cedex, France
Véronique Arnoult-Delest
Affiliation:
DANONE Research, RD 128, 91767 Palaiseau Cedex, France
Denis Pâquet
Affiliation:
DANONE Research, RD 128, 91767 Palaiseau Cedex, France
Gérard Brulé
Affiliation:
Inra-Agrocampus Rennes, UMR1253, Science et Technologie du Lait et de l'Œuf, 65 rue de St Brieuc, F-35 042 Rennes cedex, France
Marie H Famelart*
Affiliation:
DANONE Research, RD 128, 91767 Palaiseau Cedex, France
*
*For correspondence; e-mail: marie-helene.famelart@rennes.inra.fr

Abstract

The aim of the present study was to identify the nature of bonds established between protein particles after stirring that are responsible for the texture improvement of stirred yoghurts, called rebodying. Using a constant model yoghurt at pH 4·4, the effects of changes in the physicochemical conditions at stirring were studied on the subsequent rebodying. Short term rebodying was measured as the changes in viscoelastic properties at 4°C during 20 h after stirring, while long-term rebodying was measured as the viscosity changes during 28 d storage at 4°C. Moreover, stirred gels obtained from either set gels that were allowed time or not for ionic equilibration were compared. Increasing or decreasing ionic strength did not change the properties of stirred gels. Calcium chloride addition significantly decreased G′0 h, G′20 h and tan20 h but did not induce changes in the gel microstructure as observed by confocal scanning microscopy. Yoghurt rebodying could not be explained by fulfilling ionic equilibrium. Moreover, N-ethyl maleimide addition had no effect on the stirred yoghurt. Attractive electrostatic and disulphide interactions were not involved in the gel rebodying and increasing calcium concentration in the set gel limited rebodying.

Type
Research Article
Copyright
Copyright © Proprietors of Journal of Dairy Research 2008

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