patches within the whey microbead. As the whey protein was denatured
by the heating step the hydrophobic patches of the whey protein
are likely to be exposed and available for potential interaction
with riboflavin. The addition of calcium chloride would have increased
the polarity of the aqueous phase, which from Fig. 2 appears
to have created an additional driving force for the uptake of
riboflavin from the surrounding solution into the microbead, which
suggests the possibility of a hydrophobic interaction. Other studies
in the literature have reported hydrophobic interactions between
whey proteins and riboflavin. The binding of riboflavin to bovine
serum albumin was reported as being spontaneous and being
mainly entropy driven, with hydrophobic interactions playing a
key role in the interaction (Guo, Sun, & Xu, 2009).