Characterization of protein aggregates following a heating and freezing process

Katarzyna Kajak-Siemaszko (1) , Laurent Aubry (2) , Frederic Peyrin (2) , Marie-Laure Bax (3, 2) , Philippe Gatellier (2) , Thierry Astruc (2) , W. Przybylski (4) , D. Jaworsk (4) , Brigitte Gaillard-Martinie (5) , Véronique Santé-Lhoutellier (2)

1 Faculty of Human Nutrition
2 QuaPA - Qualité des Produits Animaux
3 TANDEM - Tissus animaux, nutrition, digestion, écosystème et métabolisme
4 Faculty of Human Nutrition and Consumer Sciences
5 MIC - Unité de Microbiologie

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.

Mots clés: image analysis; scanning electron microscopy; protein aggregation; freezing and heating treatment; light scattering; food science and technology

Domaines: Sciences du Vivant [q-bio]

Katarzyna Kajak-Siemaszko, Laurent Aubry, Frederic Peyrin, Marie-Laure Bax, Philippe Gatellier, et al.. Characterization of protein aggregates following a heating and freezing process. Food Research International, 2011, 44 (10), pp.3160-3166. ⟨10.1016/j.foodres.2011.07.043O⟩. ⟨hal-01191075⟩