Heat-Induced Gelation of Chicken Pectoralis Major Myosin and β-Lactoglobulin

• Published in: Journal of agricultural and food chemistry Vol. 49; no. 3; pp. 1587 - 1594
• Main Authors: Vittayanont, Manee, Vega-Warner, Virginia, Steffe, James F, Smith, Denise M
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01.03.2001
• Subjects: Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts; Animals; Biological and medical sciences; Calorimetry, Differential Scanning; Chickens; Food industries; Fundamental and applied biological sciences. Psychology; Gels; Hot Temperature; Lactoglobulins - chemistry; Meat; Muscle, Skeletal - chemistry; Myosins - chemistry; Protein Denaturation; Thermodynamics; Temperature; Heat treatment; Induction; Denaturation; Gelation; Sodium Phosphates; Aggregation; Vertebrata; Storage; Lactoglobulins; Myosin; Animal protein; Application method; Aves; Whey protein; Saline solution; Rheological properties; Sodium Chlorides
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/jf000774z

The denaturation, aggregation, and rheological properties of chicken breast muscle myosin, β-lactoglobulin (β-LG), and mixed myosin/β-LG solutions were studied in 0.6 M NaCl, 0.05 mM sodium phosphate buffer, pH 7.0, during heating. The endotherm of a mixture of myosin and β-LG was identical to that expected if the endotherm of each protein was overlaid on the same axis. The maximum aggregation rate (AR max) increased, and the temperature at the AR max (T max) and initial aggregation temperature (T o) decreased as the concentration of both proteins was increased. The aggregation profile of <0.5% myosin was altered by the presence of 0.25% β-LG. Addition of 0.5−3.0% β-LG decreased storage moduli of 1% myosin between 55 and 75 °C, but increased storage moduli (G‘) when heated to 90 °C and after cooling. β-LG had no effect on the gel point of ≥1.0% myosin, but enhanced gel strength when heated to 90 °C and after cooling. After cooling, the G‘ of 1% myosin/2%β-LG gels was about 1.7 times greater than that of gels prepared from 2% myosin/1% β-LG. Keywords: β-lactoglobulin; myosin; gelation; aggregation; denaturation