Secondary structural changes of glycinin during film and gel formation were
studied by infrared spectroscopy. Two complementary data treatments-i.e.,
principal component analysis and two-dimensional correlation spectroscopy-w
ere applied to the infrared spectra in order to determine the time evolutio
n of conformational changes. Kinetic curves, assessed by taking scores of t
he first principal components into account, revealed more pronounced change
s in the case of film formation. The development of aggregates in film and
gel, through intermolecular beta -sheets, was identified by an increase of
the absorbance band at around 1620 cm(-1). Two-dimensional infrared correla
tion spectroscopy made it possible to observe a decrease in both alpha -hel
ices and disordered structures prior to the appearance of aggregates. Chang
es in intramolecular beta -sheets took place in a second step. The more dra
stic changes observed in the case of film formation were believed to result
from dehydration and aggregation coupled phenomena.