This study investigated the effects of ultrasound-assisted thermo-alkali modification on the molecular structure of peanut protein. Further, the preparation conditions involved in embedding curcumin by the modified pea protein were also studied. It was found that within the pH range of 7 < pH < 11, with an increase in pH, the content of free sulfhydryl group in peanut protein isolate gradually increased from 10.35 ± 0.63 μmol/g (pH = 7) to 18.26 ± 0.93 μmol/g (pH = 10); and the content of disulfide bonds decreased from 44.62 ± 0.48 μmol/g (pH = 7) to 34.26 ± 2.03 μmol/g (pH = 11). In the ultrasonic power range (P < 300 W), with an increase in power, the content of free mercapto group in peanut protein isolate gradually increased from 12.44 ± 0.73 μmol/g to 19.46 ± 0.24 μmol/g (P = 250 W); and the content of disulfide bonds decreased from 42.29 ± 1.24 μmol/g to 33.28 ± 0.64 μmol/g (P = 300 W). Within the temperature range of 70 °C < T < 90 °C, with an increase in temperature, the content of free sulfhydryl group in peanut protein isolate gradually increased from 10.35 ± 0.94 μmol/g (T = 70 °C) to 19.67 ± 0.68 μmol/g (T = 90 °C), and the content of disulfide bonds decreased from 45.02 ± 2.84 μmol/g (T = 70 °C) to 34.26 ± 2.03 μmol/g (T = 90 °C). Response surface test was used to optimize the preparation conditions of nanoparticles from curcumin. The results showed that the optimum parameters of ultrasonic-assisted modification of peanut protein embedding curcumin were pH = 9.8, heating temperature T = 90 °C, ultrasonic power Q = 225 W, and heating time S = 21 min. Under these conditions, the embedding rate of curcumin reached 83.27 + 1.06%, the ABTS+ scavenging activity generally decreases with time over the 2 days period measured in PPI solution and PPI nanoparticles (PPN), the ABTS+ scavenging activity decreased from 40.8%, 52.2% and 67.3% to 27.1%, 39.0% and 60.5%, respectively. Compared with pure curcumin, the antioxidant activity was increased at presence of PPI.
Keywords: Curcumin embedding rate; Disulfide bond; Protein modification; Thiol group; Ultrasound power.
© Association of Food Scientists & Technologists (India) 2019.