Gelation of Chicken Pectoralis Major Myosin And Heat-Denatured β-Lactoglobulin

• Published in: Journal of agricultural and food chemistry 2003-01, Vol.51 (3), p.760-765
• Main Authors: Vittayanont, Manee, Steffe, James F, Flegler, Stanley L, Smith, Denise M
• Format: Article
• Language: English
• Subjects: Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts; Animals; Biological and medical sciences; Chemical Phenomena; Chemistry, Physical; Chickens; Food industries; Fundamental and applied biological sciences. Psychology; Gels; Hot Temperature; Hydrogen-Ion Concentration; Lactoglobulins - chemistry; Lactoglobulins - ultrastructure; Microscopy, Electron, Scanning; Muscle, Skeletal - chemistry; Myosins - chemistry; Myosins - ultrastructure; Poultry Products; Protein Denaturation; Rheology; Thermodynamics
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/jf020413e

Thermal, rheological, and microstructural properties of myosin (1 and 2% protein) were compared to mixtures of 1% myosin and 1% heat-denatured β-lactoglobulin aggregates (myosin/HDLG) and 1% myosin and 1% native β-lactoglobulin (myosin/β-LG) in 0.6 M NaCl and 0.05 M sodium phosphate buffer, pH 6.0, 6.5, and 7.0 during heating to 71 °C. Thermal denaturation patterns of myosin and myosin/HDLG were similar except for the appearance of an endothermic peak at 54−56 °C in the mixed system. At pH 7.0, 2% myosin began to gel at 48 °C and had a storage modulus (G‘) of 500 Pa upon cooling. Myosin/HDLG (2% total protein) had a gel point of 48 °C and a G‘ of 650 Pa, whereas myosin/β-LG had a gel point of 49 °C but the G‘ was lower (180 Pa). As the pH was decreased, the gel points of myosin and myosin/HDLG decreased and the G‘ after cooling increased. The HDLG was incorporated within the myosin gel network, whereas β-LG remained soluble. Keywords: β-Lactoglobulin; gelation; myosin; aggregates; microstructure; rheology