posted on 2021-05-24, 17:08authored byHarrison Helmick, Hazal Turasan, Merve Yildirim, Arun Bhunia, Andrea Liceaga, Jozef L. Kokini
Protein structure can be altered
with heat, but models which predict
denaturation show that globular proteins also spontaneously unfold
at low temperatures through cold denaturation. By an analysis of the
primary structure of pea protein using bioinformatic modeling, a mechanism
of pea protein cold denaturation is proposed. Pea protein is then
fractionated into partially purified legumin and vicilin components,
suspended in ethanol, and subjected to low temperatures (−10
to −20 °C). The structural characterizations of the purified
fractions are conducted through FTIR, ζ potential, dynamic light
scattering, and oil binding, and these are compared to the results
of commercial protein isolates. The observed structural changes suggest
that pea protein undergoes changes in structure as the result of low-temperature
treatments, which could lead to innovative industrial processing techniques
for functionalization by low-temperature processing.