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Purification and Characterization of Antioxidant Peptides From Enzymatically Hydrolyzed Chicken Egg White

Purification and Characterization of Antioxidant Peptides From Enzymatically Hydrolyzed Chicken Egg White

Chamila Nimalaratne, Nandika Bandara, Jianping Wu

Food Chem. 2015 Dec 1;188:467-72.

PMID: 26041219

Abstract:

Egg white is considered as a rich source of high quality proteins with various bioactive peptide fractions. Enzymatic hydrolysis of proteins can be used to release bioactive fractions and different enzymes have different abilities in releasing such bioactive fractions depending on the enzyme's site of activity on a protein. In this study, several proteases were examined for their ability to release antioxidant peptides from hen egg white and protease P was selected based on the antioxidant activity and the digestion yield of the crude protein hydrolysate. A combination of several purification steps including ultrafiltration with low molecular weight cut-off membranes, cation exchange chromatography and reversed phase high performance liquid chromatography was used to purify 'protease P egg white hydrolysate'. Sixteen antioxidant peptides, which were derived from ovalbumin, ovotransferrin and cystatin were isolated from the most active fractions. Amino acid sequences of those peptides were determined using LC-MS/MS. Oxygen radical absorbance capacity (ORAC) values of selected short chain peptides were determined using synthetic peptides. Two peptides AEERYP and DEDTQAMP (Ala-Glu-Glu-Arg-Tyr-Pro and Asp-Glu-Asp-Thr-Gln-Ala-Met-Pro) showed the highest ORAC values. The results from this study indicate that egg white is rich in antioxidant peptides which can be used as a potential source for preparing bioactive ingredients using enzymatic hydrolysis followed by purification techniques.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP81989959	Cystatin from chicken egg white		81989-95-9	Price
AP9006591	Albumin from chicken egg white		9006-59-1	Price

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