Enzymatic Hydrolysis of Ovotransferrin and the Functional Properties of Its Hydrolysates

Bioactive peptides have great potentials as nutraceutical and pharmaceutical agents that can improve human health. The objectives of this research were to produce functional peptides from ovotransferrin, a major egg white protein, using single enzyme treatments, and to analyze the properties of the hydrolysates produced. Lyophilized ovotransferrin was dissolved in distilled water at 20 mg/mL, treated with protease, elastase, papain, trypsin, or α-chymotrypsin at 1% (w/v) level of substrate, and incubated for 0-24 hours at the optimal temperature of each enzyme (protease 55 ºC, papain 37 ºC, elastase 25 ºC, trypsin 37 ºC, α-chymotrypsin 37 ºC).[CN1]  The hydrolysates were tested for antioxidant, metal-chelating, and antimicrobial activities. Protease, papain, trypsin, and α-chymotrypsin hydrolyzed ovotransferrin relatively well after 3 hours of incubation, but it took 24 hours with elastase to reach a similar degree of hydrolysis. The hydrolysates obtained after 3 hours of incubation with protease, papain, trypsin, α-chymotrypsin, and after 24 hours with elastase were selected as the best products to analyze their functional properties. None of the hydrolysates exhibited antioxidant properties in the oil emulsion nor antimicrobial property at 20 mg/mL concentration. However, ovotransferrin with α-chymotrypsin and with elastase had higher Fe³⁺-chelating activities (1.06±0.88%, 1.25±0.24%) than the native ovotransferrin (0.46±0.60%). Overall, the results indicated that the single-enzyme treatments of ovotransferrin were not effective to produce peptides with antioxidant, antimicrobial, or Fe³⁺-chelating activity. Further research on the effects of enzyme combinations may be needed.