Enzymatic hydrolysis of ovomucin an

Enzymatic hydrolysis of ovomucin and the functional and structural characteristics of peptides in the hydrolysates


Ovomucin was hydrolyzed using enzymes or by heating under alkaline conditions (pH 12.0), and the
functional, structural and compositional characteristics of the peptides in the hydrolysates were determined.
Among the treatments, heating at 100 C for 15 min under alkaline conditions (OM) produced
peptides with the highest iron-binding and antioxidant capacities. Ovomucin hydrolyzed with papain
(OMPa) or alcalase (OMAl) produced peptides with high ACE-inhibitory activity. The mass spectrometry
analysis indicated that most of the peptides from OMPa were 2 kDa. OMAl hydrolyzed ovomucin almost completely and no peptides within 700–5000 Da were
found in the hydrolasate. The results indicated that the number and size of peptides were closely related
to the functionality of the hydrolysates. Considering the time, cost and activities of the hydrolysates, OM
was the best treatment for hydrolyzing ovomucin to produce functional peptides