Combining phenolic grafting and laccase-catalyzed cross-linking: Effects on structures, technofunctional properties and human immunoglobulin E binding capacity of egg white proteins. (1st September 2021)
- Record Type:
- Journal Article
- Title:
- Combining phenolic grafting and laccase-catalyzed cross-linking: Effects on structures, technofunctional properties and human immunoglobulin E binding capacity of egg white proteins. (1st September 2021)
- Main Title:
- Combining phenolic grafting and laccase-catalyzed cross-linking: Effects on structures, technofunctional properties and human immunoglobulin E binding capacity of egg white proteins
- Authors:
- Li, Mingqin
Karboune, Salwa
Liu, Lan
Light, Kelly
L'Hocine, Lamia
Achouri, Allaoua
Pitre, Mélanie
Mateo, Cesar - Abstract:
- Highlights: Laccase-catalyzed cross-linking is an efficient approach for protein modification. Protein/ferulic acid (FA)-grafting enhances the protein cross-linking by laccase. Cross-linked products of lysozyme/ovalbumin can be modulated by attached FA sites. Polymerized lysozyme and oligomerized ovalbumin (n > 5) were obtained. Enhanced protein functionality and lower IgE binding were achieved. Abstract: The efficiency of laccase-catalyzed protein cross-linking can be impacted by substrate protein structure and competing reactions. In this study, chemical grafting of ferulic acid (FA) on protein surface was applied to modulate the cross-linking of two inflexible globular proteins, lysozyme (LZM) and ovalbumin (OVA). The extent of FA-grafting was positively correlated with protein cross-linking extent, and determined the molecular weight profile and structures of the cross-linked product. While laccase-catalyzed reactions (with or without free FA mediator) did not lead to evident cross-linking of the native proteins, oligomeric (up to 16.4%), polymeric (up to 30.6%) FA-LZMs and oligomeric FA-OVA (5.1–31.1%) were obtained upon the enzymatic treatments. The cross-linking on the grafted FA sites occurred mainly through the formation of 8–5′-noncyclic-dehydro-diferulic linkages. The effects of investigated cross-linking approach on the emulsifying, foaming properties and the immunoglobulin E (IgE) binding capacity of LZM and OVA were also evaluated in relation to the structuralHighlights: Laccase-catalyzed cross-linking is an efficient approach for protein modification. Protein/ferulic acid (FA)-grafting enhances the protein cross-linking by laccase. Cross-linked products of lysozyme/ovalbumin can be modulated by attached FA sites. Polymerized lysozyme and oligomerized ovalbumin (n > 5) were obtained. Enhanced protein functionality and lower IgE binding were achieved. Abstract: The efficiency of laccase-catalyzed protein cross-linking can be impacted by substrate protein structure and competing reactions. In this study, chemical grafting of ferulic acid (FA) on protein surface was applied to modulate the cross-linking of two inflexible globular proteins, lysozyme (LZM) and ovalbumin (OVA). The extent of FA-grafting was positively correlated with protein cross-linking extent, and determined the molecular weight profile and structures of the cross-linked product. While laccase-catalyzed reactions (with or without free FA mediator) did not lead to evident cross-linking of the native proteins, oligomeric (up to 16.4%), polymeric (up to 30.6%) FA-LZMs and oligomeric FA-OVA (5.1–31.1%) were obtained upon the enzymatic treatments. The cross-linking on the grafted FA sites occurred mainly through the formation of 8–5′-noncyclic-dehydro-diferulic linkages. The effects of investigated cross-linking approach on the emulsifying, foaming properties and the immunoglobulin E (IgE) binding capacity of LZM and OVA were also evaluated in relation to the structural properties of cross-linked proteins. … (more)
- Is Part Of:
- Food chemistry. Volume 355(2021)
- Journal:
- Food chemistry
- Issue:
- Volume 355(2021)
- Issue Display:
- Volume 355, Issue 2021 (2021)
- Year:
- 2021
- Volume:
- 355
- Issue:
- 2021
- Issue Sort Value:
- 2021-0355-2021-0000
- Page Start:
- Page End:
- Publication Date:
- 2021-09-01
- Subjects:
- Lysozyme -- Ovalbumin -- Ferulic acid-modified proteins -- Laccase -- Oxidative cross-linking -- Structural properties -- Functionalities -- IgE binding
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2021.129587 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 25623.xml