Animal Products

Enzymatic Hydrolysis of Ovomucin and the Functional and Structural Characteristics of Peptides in the Hydrolysates

Authors
  • Sandun Abeyrathne (Iowa State University)
  • Hyun yong Lee (Iowa State University)
  • Dong Uk Uk Ahn (Iowa State University)

Abstract

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 oC for 15 minutes 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, but peptides from OMTr and OM were > 2 kDa. OMAl hydrolyzed ovomucin almost completely and no peptides within 700-5,000 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.

How to Cite:

Abeyrathne, S., Lee, H. & Ahn, D. U., (2017) “Enzymatic Hydrolysis of Ovomucin and the Functional and Structural Characteristics of Peptides in the Hydrolysates”, Iowa State University Animal Industry Report 14(1). doi: https://doi.org/10.31274/ans_air-180814-374

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Published on
01 Jan 2017
Peer Reviewed