Effect of combined heat and high-pressure treatments on the texture of chicken breast muscle (pectoralis fundus).
Commercially supplied chicken breast muscle was subjected to simultaneous heat and pressure treatments. Treatment conditions ranged from ambient temperature to 70 degrees C and from 0.1 to 800 MPa, respectively, in various combinations. Texture profile analysis (TPA) of the treated samples was performed to determine changes in muscle hardness. At treatment temperatures up to and including 50 degrees C, heat and pressure acted synergistically to increase muscle hardness. However, at 60 and 70 degrees C, hardness decreased following treatments in excess of 200 MPa. TPA was performed on extracted myofibrillar protein gels that after treatment under similar conditions revealed similar effects of heat and pressure. Differential scanning calorimetry analysis of whole muscle samples revealed that at ambient pressure the unfolding of myosin was completed at 60 degrees C, unlike actin, which completely denatured only above 70 degrees C. With simultaneous pressure treatment at >200 MPa, myosin and actin unfolded at 20 degrees C. Unfolding of myosin and actin could be induced in extracted myofibrillar protein with simultaneous treatment at 200 MPa and 40 degrees C. Electrophoretic analysis indicated high pressure/temperature regimens induced disulfide bonding between myosin chains.
Zamri
Amir I
AI
School of Food Biosciences, The University of Reading, P.O. Box 226, Whiteknights, Reading RG6 6AP, UK.
Ledward
Dave A
DA
Frazier
Richard A
RA
D000818:Animals; D002152:Calorimetry, Differential Scanning; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D005511:Food Handling / Q000379:methods*; D006358:Hot Temperature; D008460:Meat; D009124:Muscle Proteins / Q000737:chemistry; D018482:Muscle, Skeletal; D009210:Myofibrils / Q000737:chemistry; D011312:Pressure; D012677:Sensation
D009124:Muscle Proteins