کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
6405380 | 1330916 | 2012 | 8 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Dynamic rheology and endothermic transitions of proteins recovered from chicken-meat processing by-products using isoelectric solubilization/precipitation and addition of TiO2 Dynamic rheology and endothermic transitions of proteins recovered from chicken-meat processing by-products using isoelectric solubilization/precipitation and addition of TiO2](/preview/png/6405380.png)
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, Gâ²), 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 (Gâ²) generally increased when TiO2 was added to the ISP-recovered proteins. Gels made of chicken breast had the highest (PÂ <Â 0.05) shear stress (i.e., gel strength), but gels made of the ISP-recovered chicken proteins had greater (PÂ <Â 0.05) shear strain (i.e., gel cohesiveness). Addition of TiO2 to the ISP-recovered proteins resulted in increased (PÂ <Â 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.
⺠Functional protein isolate was recovered from skin-on bone-in chicken drumsticks. ⺠TiO2 improved endothermic transitions and gelation of ISP-recovered proteins. ⺠Shear stress but not strain of ISP breast gels was higher than ISP drumstick gels.
Journal: LWT - Food Science and Technology - Volume 46, Issue 1, April 2012, Pages 148-155