Fibril for
mation in
mixtures of whey proteins upon heating at pH 2 was investigated. Fibrils werefound to
coexist with other stru
ctures, su
ch as spherulites. These spherulites
consist of radially orientedfibrils. At total protein
con
centrations above 6 wt %, transparent gels were for
med. Changing theratio between the various whey proteins did not affe
ct this gelation
con
centration as long as
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mages/gif
chars/beta2.gif" BORDER=0 ALIGN="
middle">-la
ctoglobulin (
![](/i<font color=)
mages/gif
chars/beta2.gif" BORDER=0 ALIGN="
middle">-lg) was present, suggesting that
![](/i<font color=)
mages/gif
chars/beta2.gif" BORDER=0 ALIGN="
middle">-lg was do
minant in the gelation. Pure
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chars/alpha.gif" BORDER=0>-la
ctalbu
min and pure bovine seru
m albu
min did not for
m fibrils, nor did they gel upon heating atpH 2 and 80
![](/i<font color=)
mages/entities/deg.gif">C for up to 10 h. They did however indu
ce a de
crease in the
![](/i<font color=)
mages/gif
chars/beta2.gif" BORDER=0 ALIGN="
middle">-lg
con
centration neededfor gel for
mation upon heating at pH 2. Our results suggest that
![](/i<font color=)
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chars/beta2.gif" BORDER=0 ALIGN="
middle">-lg is the only fibril for
ming proteinat the
conditions used and that no
mixed fibrils are for
med.Keywords: Heat-indu
ced aggregation; heat-set gelation; fibrils; whey proteins;
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chars/beta2.gif" BORDER=0 ALIGN="
middle">-la
ctoglobulin