title: Thermal denaturation and aggregation properties of Atlantic salmon myofibrils and myosin from white and red muscles.
abstract: Thermal denaturation and aggregation abilities of salmon myofibrils and myosin were studied measuring turbidity, intrinsic fluorescence, 8-anilino-1-naphthalene 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.
authors.affiliation: INRA SCRIBE, Group Growth and Quality, IFR 140, Campus de Beaulieu, 35000 Rennes, France. Florence.Lefevre@rennes.inra.fr
authors.forename: Florence
authors.initials: F
authors.lastname: Lefevre
authors.forename: Benoit
authors.initials: B
authors.lastname: Fauconneau
authors.forename: John W
authors.initials: JW
authors.lastname: Thompson
authors.forename: Tom A
authors.initials: TA
authors.lastname: Gill
mesh_terms: D000817:Anilino Naphthalenesulfonates; D000818:Animals; D003432:Cross-Linking Reagents; D005456:Fluorescent Dyes; D005782:Gels; D006358:Hot Temperature; D049449:Luminescence; D018656:Muscle Fibers, Fast-Twitch / Q000737:chemistry*; D009124:Muscle Proteins / Q000032:analysis / Q000737:chemistry*; D018482:Muscle, Skeletal / Q000737:chemistry*; D009210:Myofibrils / Q000737:chemistry*; D009218:Myosins / Q000737:chemistry*; D009391:Nephelometry and Turbidimetry; D011489:Protein Denaturation; D020317:Salmo salar; D013816:Thermodynamics
chemical_list: D000817:Anilino Naphthalenesulfonates; D003432:Cross-Linking Reagents; D005456:Fluorescent Dyes; D005782:Gels; D009124:Muscle Proteins; C027132:1-anilino-8-naphthalenesulfonate; D009218:Myosins