Thermal Denaturation and Aggregation Properties of Atlantic Salmon Myofibrils and Myosin from White and Red Muscles

• DOI: 10.1021/jf063045d
• Publication Date: 2007-05-12T11:00:46Z
• Authors: Florence Lefevre; Benoit Fauconneau; John W. Thompson; Tom A. Gill
• Keywords: Myofibril; Denaturation (fissile materials); Meromyosin

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