Comparative Composition and Antioxidant Activity of Peptide Fractions Obtained by Ultrafiltration of Egg Yolk Protein Enzymatic Hydrolysates
The objective of the study was to compare the antioxidant activity of two distinct hydrolysates and their peptide fractions prepared by ultrafiltration (UF) using membranes with molecular weight cut-off of 5 and 1 kDa. The hydrolysates were a delipidated egg yolk protein concentrate (EYP) intensivel...
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doaj-cb7c1541f3eb49a28a65bf9bdf995cc62020-11-25T00:02:30ZengMDPI AGMembranes2077-03752011-07-011314916110.3390/membranes1030149Comparative Composition and Antioxidant Activity of Peptide Fractions Obtained by Ultrafiltration of Egg Yolk Protein Enzymatic HydrolysatesYves PouliotTsutomu OkuboLekh R. JunejaYoshinori MineBertrand P. Chay Pak TingSylvie F. GauthierThe objective of the study was to compare the antioxidant activity of two distinct hydrolysates and their peptide fractions prepared by ultrafiltration (UF) using membranes with molecular weight cut-off of 5 and 1 kDa. The hydrolysates were a delipidated egg yolk protein concentrate (EYP) intensively hydrolyzed with a combination of two bacterial proteases, and a phosphoproteins (PPP) extract partially hydrolyzed with trypsin. Antioxidant activity, as determined by the oxygen radical absorbance capacity (ORAC) assay, was low for EYP and PPP hydrolysates with values of 613.1 and 489.2 µM TE×g−1 protein, respectively. UF-fractionation of EYP hydrolysate increased slightly the antioxidant activity in permeate fractions (720.5–867.8 µM TE×g−1 protein). However, ORAC values were increased by more than 3-fold in UF-fractions prepared from PPP hydrolysate, which were enriched in peptides with molecular weight lower than 5 kDa. These UF-fractions were characterized by their lower N/P atomic ratio and higher phosphorus content compared to the same UF-fractions obtained from EYP-TH. They also contained high amounts of His, Met, Leu, and Phe, which are recognized as antioxidant amino acids, but also high content in Lys and Arg which both represent target amino acids of trypsin used for the hydrolysis of PPP.http://www.mdpi.com/2077-0375/1/3/149/egg yolk proteinsenzymatic hydrolysisultrafiltrationantioxidant activity |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yves Pouliot Tsutomu Okubo Lekh R. Juneja Yoshinori Mine Bertrand P. Chay Pak Ting Sylvie F. Gauthier |
spellingShingle |
Yves Pouliot Tsutomu Okubo Lekh R. Juneja Yoshinori Mine Bertrand P. Chay Pak Ting Sylvie F. Gauthier Comparative Composition and Antioxidant Activity of Peptide Fractions Obtained by Ultrafiltration of Egg Yolk Protein Enzymatic Hydrolysates Membranes egg yolk proteins enzymatic hydrolysis ultrafiltration antioxidant activity |
author_facet |
Yves Pouliot Tsutomu Okubo Lekh R. Juneja Yoshinori Mine Bertrand P. Chay Pak Ting Sylvie F. Gauthier |
author_sort |
Yves Pouliot |
title |
Comparative Composition and Antioxidant Activity of Peptide Fractions Obtained by Ultrafiltration of Egg Yolk Protein Enzymatic Hydrolysates |
title_short |
Comparative Composition and Antioxidant Activity of Peptide Fractions Obtained by Ultrafiltration of Egg Yolk Protein Enzymatic Hydrolysates |
title_full |
Comparative Composition and Antioxidant Activity of Peptide Fractions Obtained by Ultrafiltration of Egg Yolk Protein Enzymatic Hydrolysates |
title_fullStr |
Comparative Composition and Antioxidant Activity of Peptide Fractions Obtained by Ultrafiltration of Egg Yolk Protein Enzymatic Hydrolysates |
title_full_unstemmed |
Comparative Composition and Antioxidant Activity of Peptide Fractions Obtained by Ultrafiltration of Egg Yolk Protein Enzymatic Hydrolysates |
title_sort |
comparative composition and antioxidant activity of peptide fractions obtained by ultrafiltration of egg yolk protein enzymatic hydrolysates |
publisher |
MDPI AG |
series |
Membranes |
issn |
2077-0375 |
publishDate |
2011-07-01 |
description |
The objective of the study was to compare the antioxidant activity of two distinct hydrolysates and their peptide fractions prepared by ultrafiltration (UF) using membranes with molecular weight cut-off of 5 and 1 kDa. The hydrolysates were a delipidated egg yolk protein concentrate (EYP) intensively hydrolyzed with a combination of two bacterial proteases, and a phosphoproteins (PPP) extract partially hydrolyzed with trypsin. Antioxidant activity, as determined by the oxygen radical absorbance capacity (ORAC) assay, was low for EYP and PPP hydrolysates with values of 613.1 and 489.2 µM TE×g−1 protein, respectively. UF-fractionation of EYP hydrolysate increased slightly the antioxidant activity in permeate fractions (720.5–867.8 µM TE×g−1 protein). However, ORAC values were increased by more than 3-fold in UF-fractions prepared from PPP hydrolysate, which were enriched in peptides with molecular weight lower than 5 kDa. These UF-fractions were characterized by their lower N/P atomic ratio and higher phosphorus content compared to the same UF-fractions obtained from EYP-TH. They also contained high amounts of His, Met, Leu, and Phe, which are recognized as antioxidant amino acids, but also high content in Lys and Arg which both represent target amino acids of trypsin used for the hydrolysis of PPP. |
topic |
egg yolk proteins enzymatic hydrolysis ultrafiltration antioxidant activity |
url |
http://www.mdpi.com/2077-0375/1/3/149/ |
work_keys_str_mv |
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