Abstract
The mulberry leaf protein extracted by ultrasound-assisted cellulase degradation (UACD) method was optimized with the protein dissolution amount (PDA) as the index. The Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy of extracted mulberry leaf protein were measured. The functional characteristics of protein extracted by the UACD method were evaluated. Results showed that the extraction condition was optimized and adjusted to the following parameters: pH value of 7.20, ultrasound temperature of 35.00 °C, enzyme dosage of 4.20% and ultrasound time of 10.00 min. Under these optimized conditions, the experimental verification value of PDA was 13.87 mg/mL, which was approaching to the predicted value of 13.54 mg/mL. The analysis results of FTIR showed that after extraction by the UACD method, the mulberry leaf protein with the vibrational peak of ester carbonyl (C = O) absorption peak (1734.66 cm(-1)) disappeared. The α-helix content of protein extracted by the UACD decreased by 8.13%, and the β-turn and random coil content of protein increased by 20.22% and 18.79%, respectively, compared to that of the blank. The microstructure of mulberry leaf protein showed that the UACD method could break the dense structure of protein raw materials, reduce the average size of proteins and increase the specific surface area and roughness of proteins. According to the results of functional characteristics, the mulberry leaf protein extracted by the UACD method presented the highest enzymolysis properties and solubility, which was beneficial for the application in the food industry. In conclusion, the UACD method was a very effective way to extract protein from mulberry leaf.