Acid gelation properties of heated skim milk as a result of enzymatically induced changes in the micelle/serum distribution of the whey protein/kappa-casein aggregates.
Changes in the acid gelation properties of skim milk as a result of variations in the micelle/serum distribution of the heat-induced whey protein/kappa-casein aggregates, induced by the combination of heat treatment and limited renneting, were investigated. No dramatic change in the zeta potential or the isoelectric point of the casein micelles was suggested, whether the aggregates were all attached to the casein micelle or not. Fluorescence intensity measurement using 8-anilino-1-naphthalenesulfonic acid (ANS) showed that the heat-induced aggregates were highly hydrophobic. Dynamic oscillation viscosimetry showed that acid gelation using glucono-delta-lactone (GDL) started at a higher pH value in prerenneted milk. However, no change in the gelation profile of skim milk could be related to the proportion of aggregates bound to the surface of the casein micelles. The results support the idea of an early interaction between the serum aggregates and the casein micelles on acidification.
INRA-Agrocampus Rennes, UMR 1253, Science et Technologie du Lait et de l'CEuf, Rennes, France. fanny.guyomarch@rennes.inra.fr
Fanny
F
Guyomarc'h
Marie
M
Renan
Marc
M
Chatriot
Valérie
V
Gamerre
Marie-Hélène
MH
Famelart
D000818:Animals; D002364:Caseins / Q000737:chemistry / Q000378:metabolism*; D012085:Chymosin / Q000378:metabolism*; D005782:Gels / Q000737:chemistry*; D006358:Hot Temperature; D057927:Hydrophobic and Hydrophilic Interactions; D007526:Isoelectric Point; D008823:Micelles; D008892:Milk / Q000737:chemistry*; D008894:Milk Proteins / Q000737:chemistry / Q000378:metabolism*; D000067816:Whey Proteins
D002364:Caseins; D005782:Gels; D008823:Micelles; D008894:Milk Proteins; D000067816:Whey Proteins; C025350:rennet; D012085:Chymosin