Characterization of protein aggregates following a heating and freezing process

Abstract This study used complementary multi-scale analytical methods in order to better understand how technological procedures such as freezing and heating affect protein aggregation. The research was conducted on fresh and frozen Longissimus dorsi (LD) which were heated at different temperatures and for various times. Protein aggregates were measured using light scattering, SDS PAGE electrophoresis, and optical and scanning electron microscopy. Heating led to a higher molecular weight of aggregates, while freezing had an additive effect on aggregates, with the actin band decreasing as cooking times increased.