title: Enzymatic hydrolysis of ovomucoid and the functional properties of its hydrolysates.
abstract: 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.
authors.affiliation: Department of Animal Science, Uva Wellassa University, Badulla, Sri Lanaka 90000.
authors.forename: E D N S
authors.initials: ED
authors.lastname: Abeyrathne
authors.affiliation: Department of Animal Science, Iowa State University, Ames, IA 50011, USA.
authors.forename: H Y
authors.initials: HY
authors.lastname: Lee
authors.affiliation: Department of Animal Science, Iowa State University, Ames, IA 50011, USA.
authors.forename: C
authors.initials: C
authors.lastname: Jo
authors.affiliation: Center for Nutraceutical and Pharmaceutical Materials, Myongji University, Cheoin-gu, Yongin, Gyeonggi-Do 449-728, Korea duahn@iastate.edu jwsuh@mju.ac/kr.
authors.forename: J W
authors.initials: JW
authors.lastname: Suh
authors.affiliation: Department of Animal Science, Iowa State University, Ames, IA 50011, USA Department of Animal Science and Technology, Sunchon National University, Sunchon 540-742, South Korea duahn@iastate.edu jwsuh@mju.ac/kr.
authors.forename: D U
authors.initials: DU
authors.lastname: Ahn
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000032:analysis; D000818:Animals; D000975:Antioxidants / Q000032:analysis; D030161:Avian Proteins / Q000737:chemistry* / Q000378:metabolism*; D002614:Chelating Agents / Q000032:analysis; D002645:Chickens / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism; D006868:Hydrolysis; D008670:Metals / Q000737:chemistry; D010059:Ovomucin / Q000737:chemistry* / Q000378:metabolism*; D010063:Ovum / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D053719:Tandem Mass Spectrometry
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D000975:Antioxidants; D030161:Avian Proteins; D002614:Chelating Agents; D008670:Metals; D010455:Peptides; D010059:Ovomucin; D010450:Endopeptidases
keywords: Ovomucoid; enzyme hydrolysis; functional properties; peptides