Advances in Understanding the Antioxidant and Antigenic Properties of Egg-Derived Peptides
Pepsin, trypsin and proteinase K were used in the present study to hydrolyse the proteins from whole eggs, yolks or whites, and the resulting hydrolysates were characterised in terms of antioxidant and IgE-binding properties, using a combination of in vitro and in silico methods. Based on the degree...
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| Language: | English |
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MDPI AG
2024-03-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/29/6/1327 |
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| author | Mihaela Brumă (Călin) Ina Vasilean Leontina Grigore-Gurgu Iuliana Banu Iuliana Aprodu |
| author_facet | Mihaela Brumă (Călin) Ina Vasilean Leontina Grigore-Gurgu Iuliana Banu Iuliana Aprodu |
| author_sort | Mihaela Brumă (Călin) |
| collection | DOAJ |
| description | Pepsin, trypsin and proteinase K were used in the present study to hydrolyse the proteins from whole eggs, yolks or whites, and the resulting hydrolysates were characterised in terms of antioxidant and IgE-binding properties, using a combination of in vitro and in silico methods. Based on the degree of hydrolysis (DH) results, the egg yolk proteins are better substrates for all the tested enzymes (DH of 6.2–20.1%) compared to those from egg whites (DH of 2.0–4.4%). The SDS-PAGE analysis indicated that pepsin and proteinase K were more efficient compared to trypsin in breaking the intramolecular peptide bonds of the high molecular weight egg proteins. For all the tested substrates, enzyme-assisted hydrolysis resulted in a significant increase in antioxidant activity, suggesting that many bioactive peptides are encrypted in inactive forms in the parent proteins. The hydrolysates obtained with proteinase K exhibited the highest DPPH radical scavenging activity (124–311 µM Trolox/g protein) and the lowest residual IgE-binding capacity. The bioinformatics tools revealed that proteinase K is able to break the integrity of the main linear IgE-binding epitopes from ovalbumin and ovomucoid. It can be concluded that proteinase K is a promising tool for modulating the intrinsic properties of egg proteins. |
| first_indexed | 2024-04-24T17:58:33Z |
| format | Article |
| id | doaj.art-a7674da29fee4ed7a1e913f351a9de8f |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-04-24T17:58:33Z |
| publishDate | 2024-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-a7674da29fee4ed7a1e913f351a9de8f2024-03-27T13:57:04ZengMDPI AGMolecules1420-30492024-03-01296132710.3390/molecules29061327Advances in Understanding the Antioxidant and Antigenic Properties of Egg-Derived PeptidesMihaela Brumă (Călin)0Ina Vasilean1Leontina Grigore-Gurgu2Iuliana Banu3Iuliana Aprodu4Faculty of Food Science and Engineering, Dunarea de Jos University of Galati, 111 Domneasca Street, 800201 Galati, RomaniaFaculty of Food Science and Engineering, Dunarea de Jos University of Galati, 111 Domneasca Street, 800201 Galati, RomaniaFaculty of Food Science and Engineering, Dunarea de Jos University of Galati, 111 Domneasca Street, 800201 Galati, RomaniaFaculty of Food Science and Engineering, Dunarea de Jos University of Galati, 111 Domneasca Street, 800201 Galati, RomaniaFaculty of Food Science and Engineering, Dunarea de Jos University of Galati, 111 Domneasca Street, 800201 Galati, RomaniaPepsin, trypsin and proteinase K were used in the present study to hydrolyse the proteins from whole eggs, yolks or whites, and the resulting hydrolysates were characterised in terms of antioxidant and IgE-binding properties, using a combination of in vitro and in silico methods. Based on the degree of hydrolysis (DH) results, the egg yolk proteins are better substrates for all the tested enzymes (DH of 6.2–20.1%) compared to those from egg whites (DH of 2.0–4.4%). The SDS-PAGE analysis indicated that pepsin and proteinase K were more efficient compared to trypsin in breaking the intramolecular peptide bonds of the high molecular weight egg proteins. For all the tested substrates, enzyme-assisted hydrolysis resulted in a significant increase in antioxidant activity, suggesting that many bioactive peptides are encrypted in inactive forms in the parent proteins. The hydrolysates obtained with proteinase K exhibited the highest DPPH radical scavenging activity (124–311 µM Trolox/g protein) and the lowest residual IgE-binding capacity. The bioinformatics tools revealed that proteinase K is able to break the integrity of the main linear IgE-binding epitopes from ovalbumin and ovomucoid. It can be concluded that proteinase K is a promising tool for modulating the intrinsic properties of egg proteins.https://www.mdpi.com/1420-3049/29/6/1327egg proteinsproteolytic enzymeshydrolysis degreeantioxidant activityantigenic properties |
| spellingShingle | Mihaela Brumă (Călin) Ina Vasilean Leontina Grigore-Gurgu Iuliana Banu Iuliana Aprodu Advances in Understanding the Antioxidant and Antigenic Properties of Egg-Derived Peptides Molecules egg proteins proteolytic enzymes hydrolysis degree antioxidant activity antigenic properties |
| title | Advances in Understanding the Antioxidant and Antigenic Properties of Egg-Derived Peptides |
| title_full | Advances in Understanding the Antioxidant and Antigenic Properties of Egg-Derived Peptides |
| title_fullStr | Advances in Understanding the Antioxidant and Antigenic Properties of Egg-Derived Peptides |
| title_full_unstemmed | Advances in Understanding the Antioxidant and Antigenic Properties of Egg-Derived Peptides |
| title_short | Advances in Understanding the Antioxidant and Antigenic Properties of Egg-Derived Peptides |
| title_sort | advances in understanding the antioxidant and antigenic properties of egg derived peptides |
| topic | egg proteins proteolytic enzymes hydrolysis degree antioxidant activity antigenic properties |
| url | https://www.mdpi.com/1420-3049/29/6/1327 |
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