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

被引:43
作者
Abeyrathne, E. D. N. S. [1 ]
Lee, H. Y. [2 ]
Jo, C. [3 ]
Suh, J. W. [4 ,5 ]
Ahn, D. U. [2 ]
机构
[1] Uva Wellassa Univ, Dept Anim Sci, Badulla 90000, Sri Lanka
[2] Iowa State Univ, Dept Anim Sci, Ames, IA 50011 USA
[3] Seoul Natl Univ, Dept Agr Biotechnol, Coll Agr & Life Sci, Seoul 151742, South Korea
[4] Myongji Univ, Ctr Nutraceut & Pharmaceut Mat, Yongin 449728, Gyeonggi Do, South Korea
[5] Sunchon Natl Univ, Dept Anim Sci & Technol, Sunchon 540742, South Korea
关键词
Ovomucin; Enzyme hydrolysis; Peptides; Functional properties; PRONASE-TREATED FRAGMENTS; HEN EGG-WHITE; GLYCOPEPTIDES; ANTIBODIES;
D O I
10.1016/j.foodchem.2015.06.055
中图分类号
O69 [应用化学];
学科分类号
070301 [无机化学];
摘要
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 degrees 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, but peptides from OMTr and OM 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. (C) 2015 Elsevier Ltd. All rights reserved.
引用
收藏
页码:107 / 113
页数:7
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