Enzymatic hydrolysis of ovalbumin and the functional properties of the hydrolysates

Abstract

Ovalbumin is the predominant protein in egg white and is widely used in cell culture. However, it also can be used to produce peptides with various functional properties. The objectives of this study were to hydrolyze ovalbumin using various enzyme, incubation time, and temperature combinations, and to compare the functional properties of the hydrolysates. Ovalbumin (20 mg/mL) was hydrolyzed with 1% of pepsin, trypsin, alpha-chymotrypsin, papain, and alcalase, singly or in combination at 37A degrees C, and then the enzymes were inactivated at 100A degrees C for 15 min. Hydrolyzing ovalbumin with pepsin (OAPe), pepsin + papain (OAPePa), pepsin + alcalase (OAPeAl), alcalase + trypsin (OAAlTr), and alpha-chymotrypsin (OACh) was also effective in producing peptides from ovalbumin, and the peptides produced had strong iron- and copper-binding capacities and antioxidant capability. However, the best treatment of all was the OAAlTr treatment, which showed the highest iron-chelating and antioxidant activities among the enzyme treatments (P < 0.05). Electrospray-ionization mass spectrometry (MS/MS) analysis identified numerous peptides (< 5 kDa) from the OAPe, OAPeAl, OACh, OAAlTr, and OAPePa hydrolysates of ovalbumin, but the number and size of peptides varied widely depending on the treatments. The enzymatic hydrolysis significantly increased the functionality of ovalbumin, and the improvement depended upon the composition of peptides produced rather than the number of the peptides produced.