Dynamic rheology and endothermic transitions of proteins recovered from chicken-meat processing by-products using isoelectric solubilization/precipitation and addition of TiO2 |
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Authors: | Reza Tahergorabi Litha Sivanandan Jacek Jaczynski |
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Affiliation: | 1. Animal and Nutritional Sciences, West Virginia University, PO Box 6108, Morgantown, WV, USA;2. West Virginia University Extension Service, PO Box 6031, 610 Knapp Hall, Morgantown, WV, USA |
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Abstract: | Chicken-meat processing generates large quantities of by-products (backs, necks, etc.). Dark chicken-meat processing by-products present the lowest value and greatest challenge. Therefore, recovery of functional proteins from this source for inclusion in food products resembling those from light chicken-meat presents the greatest value addition and opportunity. Novel isoelectric solubilization/precipitation (ISP) was applied to model, dark chicken-meat processing by-products (skin-on bone-in chicken drumsticks) to recover muscle proteins. Thermal denaturation (endothermic transitions), gelation (elasticity, G′), and fundamental texture properties (shear stress and strain at mechanical fracture) of the ISP-recovered proteins were determined with differential scanning calorimetry (DSC), dynamic rheometer, and torsion test, respectively; and compared to boneless skinless chicken breast. Endothermic transition of myosin was not detected only when TiO2 was not added, while the ISP-recovered proteins with TiO2 showed small myosin peak and large actin peak. However, the level of TiO2 addition did not affect thermal transition/denaturation of the ISP-recovered proteins. The ISP-recovered proteins had a greater transition for actin compared to chicken breast, suggesting that ISP predisposes this protein to thermal denaturation. Similar to endothermic transitions, elasticity (G′) generally increased when TiO2 was added to the ISP-recovered proteins. Gels made of chicken breast had the highest (P < 0.05) shear stress (i.e., gel strength), but gels made of the ISP-recovered chicken proteins had greater (P < 0.05) shear strain (i.e., gel cohesiveness). Addition of TiO2 to the ISP-recovered proteins resulted in increased (P < 0.05) gel strength. Based on the present study, addition of TiO2 is suggested for the development of restructured food products based on proteins recovered from dark chicken-meat processing by-products using ISP. Although the results of this study point towards a novel food product, further studies are recommended. |
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