Thermal denaturation and aggregation properties of Atlantic salmon myofibrils and myosin from white and red muscles

• Published in: Journal of Agricultural and Food Chemistry
• Main Authors: Lefèvre, Florence, Fauconneau, Benoit, Thompson, John W., Gill, Tom A.
• Other Authors: Station commune de Recherches en Ichtyophysiologie, Biodiversité et Environnement (SCRIBE), Institut National de la Recherche Agronomique (INRA), Dalhousie University
• Format: Article in Journal/Newspaper
• Language: English
• Published: HAL CCSD 2007
• Subjects: salmon; myosin; thermal gelation; myofibrils; muscle type; [SDV.IDA]Life Sciences [q-bio]/Food engineering; Atlantic salmon
• Online Access: https://hal.inrae.fr/hal-02662295; https://doi.org/10.1021/jf063045d

International audience Thermal denaturation and aggregation abilities of salmon myofibrils and myosin were studied measuring turbidity, intrinsic fluorescence, 8-anilino-1-naphtalene sulfonic acid binding, and 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide cross-linking. The thermal behaviors of protein preparation from white and red muscles were compared, and the relationship with thermal gelation properties is discussed. The low gelation ability of salmon muscle proteins was related to a limited extent of protein denaturation and aggregation upon heating. These properties seemed to be carried by myosin molecules as a similar behavior was observed for both myofibrils and myosin preparations. The higher thermal stability observed for red muscle proteins with higher transition temperatures in rheological profiles was related to a shift to higher temperature in denaturation and aggregation processes. The extent of denaturation and aggregation was very similar for both muscle types as was the final rigidity of the gels formed.