Thermal denaturation of hake (Merluccius hubbsi) myofibrillar proteins. A Differential Scanning Calorimetric and electrophoretic study

BEAS V.E.; WAGNER, J.R; CRUPKIN, M; AÑON, MARÍA CRISTINA

JOURNAL OF FOOD SCIENCE

WILEY-BLACKWELL PUBLISHING, INC

Lugar: Londres; Año: 1990 vol. 55 p. 683 - 687

0022-1147

Denaturation of hake (Merluccius hubbsi) proteins was studied withDSC by monitoring T,,, of transitions and denaturation enthalpies.Whole muscle free of connective tissue showed two transitions (T,,,,465°C and 75.3?C), and AH of 4.27 Cal/g. The exudative sarcoplasmic fraction showed three transitions (T,, 45.2?C, 59.O?C and75.5?C) and AH of 3.92 Cal/g. The sarcoplasmic proteins from wholehake muscle contributed to both denaturation peaks. Muscle depletedof sarcoplasmic proteins by chloride extraction showed a higher thermal sensitivity and a diminished denaturation enthalpy on the secondtransition. This suggested an additional effect of chloride upon actinin addition to sarcoplasmic protein extraction. pH had an effect uponthe native conformation of thick filament proteins, specifically myosin.