Enzymatic hydrolysis of ovomucoid and the functional properties of its hydrolysates

dc.contributor.author Abeyrathne, E. D. N. S.
dc.contributor.author Lee, H. Y.
dc.contributor.author Jo, C.
dc.contributor.author Suh, J. W.
dc.contributor.author Ahn, Dong
dc.contributor.department Animal Science
dc.date 2021-05-26T21:11:28.000
dc.date.accessioned 2021-08-14T02:08:46Z
dc.date.available 2021-08-14T02:08:46Z
dc.date.copyright Thu Jan 01 00:00:00 UTC 2015
dc.date.issued 2015-09-01
dc.description.abstract <p>Ovomucoid is well known as a “trypsin inhibitor” and is considered to be the main food allergen in egg. However, the negative functions of ovomucoid can be eliminated if the protein is cut into small peptides. The objectives of this study were to hydrolyze ovomucoid using various enzyme combinations, and compare the functional properties of the hydrolysates. Purified ovomucoid was dissolved in distilled water (20 mg/mL) and treated with 1% of pepsin, α-chymotrypsin, papain, and alcalase, singly or in combinations. Sodium sodium dodecyl sulfate-polyacrylamide (SDS-PAGE) results of the hydrolysates indicated that pepsin (OMP), alcalase (OMAl), alcalase + trypsin (OMAlTr), and alcalase + papain (OMAlPa) treatments best hydrolyzed the ovomucoid, and the 4 treatments were selected to determine their functional characteristics. Among the 4 enzyme treatments, hydrolysate from OMAlTr showed the highest iron-chelating and antioxidant activities, while OMP showed higher ACE-inhibitory activity, but lower Fe-chelating activity than the other treatments. However, no difference in the copper-chelating activity among the treatments was found. MS/MS analysis identified numerous peptides from the hydrolysates of OMAlPa and OMAlTr, and majority of the peptides produced were <2 kDa. Pepsin treatment (OMP), however, hydrolyzed ovomucoid almost completely and produced only amino acid monomers, di- and tri-peptides. The ACE-inhibitory, antioxidant and iron-chelating activities of the enzyme hydrolysates were not consistent with the number and size of peptides in the hydrolysates, but we do not have information about the quantity of each peptide present in the hydrolysates at this point.</p>
dc.description.comments <p>This article is published as Abeyrathne, E. D. N. S., H. Y. Lee, C. Jo, J. W. Suh, and D. U. Ahn. "Enzymatic hydrolysis of ovomucoid and the functional properties of its hydrolysates." <em>Poultry science</em> 94, no. 9 (2015): 2280-2287. doi:<a href="https://doi.org/10.3382/ps/pev196" target="_blank" title="Persistent link using digital object identifier">10.3382/ps/pev196</a>.</p>
dc.format.mimetype application/pdf
dc.identifier archive/lib.dr.iastate.edu/ans_pubs/871/
dc.identifier.articleid 1875
dc.identifier.contextkey 23102639
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath ans_pubs/871
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/erLKoROv
dc.language.iso en
dc.source.bitstream archive/lib.dr.iastate.edu/ans_pubs/871/0-CC_license_for_2015_Ahn_EnzymaticHydrolysis.pdf|||Sat Jan 15 02:15:58 UTC 2022
dc.source.bitstream archive/lib.dr.iastate.edu/ans_pubs/871/2015_Ahn_EnzymaticHydrolysis.pdf|||Sat Jan 15 02:15:59 UTC 2022
dc.source.uri 10.3382/ps/pev196
dc.subject.disciplines Agriculture
dc.subject.disciplines Animal Sciences
dc.subject.disciplines Poultry or Avian Science
dc.subject.keywords Ovomucoid
dc.subject.keywords enzyme hydrolysis
dc.subject.keywords peptides
dc.subject.keywords functional properties
dc.title Enzymatic hydrolysis of ovomucoid and the functional properties of its hydrolysates
dc.type article
dc.type.genre article
dspace.entity.type Publication
relation.isAuthorOfPublication d3386101-2f0d-4375-ab44-ac1addb6a9ad
relation.isOrgUnitOfPublication 85ecce08-311a-441b-9c4d-ee2a3569506f
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