Abstract
The present study investigated the impact of quinoa protein (QP) on the physicochemical properties, sensory quality, and oxidative stability of myofibrillar protein (MP) in pork patties during five freeze-thaw (F-T) cycles. It was observed that repeated F-T cycles resulted in a deterioration of pork patty quality; however, the incorporation of QP effectively mitigated these changes. Throughout the F-T cycles, the sensory quality of the QP-treated group consistently surpassed that of the control group. After five F-T cycles, the thiobarbituric acid reactive substance (TBARS) content in the control group was measured at 0.423 mg/kg, whereas it significantly decreased to 0.347 mg/kg in the QP-treated group (p < 0.05). Furthermore, QP inclusion led to a decrease in pH and an increase in water-holding capacity (WHC) within pork patties. Following five F-T cycles, Ca2+-ATPase activity exhibited a significant increase of 11.10% in the QP-treated group compared to controls (p < 0.05). Additionally, supplementation with QP resulted in elevated total sulfhydryl content and reduced carbonyl content, Schiff base content, and dityrosine content within myofibrillar proteins (MPs), indicating its inhibitory effect on MP oxidation. In particular, after five F-T cycles, total sulfhydryl content reached 58.66 nmol/mL for the QP-treated group significantly higher than that observed for controls at 43.65 nmol/mL (p < 0.05). While carbonyl content increased from 2.37 nmol/mL to 4.63 nmol/mL between the first and fifth F-T cycle for controls; it only rose from 2.15 nmol/mL to 3.47 nmol/mL in the QP-treated group. The endogenous fluorescence levels were significantly higher (p < 0.05) in the QP-treated group compared to controls. In conclusion, the addition of QP enhanced the quality of pork patties and effectively inhibited the oxidative denaturation of MP during F-T cycles.