Combining phenolic grafting and laccase-catalyzed cross-linking: Effects on structures, technofunctional properties and human immunoglobulin E binding capacity of egg white proteins
| Autor: | Mélanie Pitre, Mingqin Li, Allaoua Achouri, Lan Liu, Lamia L'Hocine, Kelly Light, Cesar Mateo, Salwa Karboune |
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| Rok vydání: | 2020 |
| Předmět: |
Coumaric Acids
Globular protein Ovalbumin 01 natural sciences Analytical Chemistry Ferulic acid Antigen-Antibody Reactions chemistry.chemical_compound 0404 agricultural biotechnology Protein structure Phenols Humans chemistry.chemical_classification Laccase biology 010401 analytical chemistry Substrate (chemistry) 04 agricultural and veterinary sciences General Medicine Immunoglobulin E 040401 food science 0104 chemical sciences Molecular Weight Enzyme Cross-Linking Reagents chemistry Biochemistry biology.protein Biocatalysis Muramidase Lysozyme Oxidation-Reduction Food Science |
| Zdroj: | Food chemistry. 355 |
| ISSN: | 1873-7072 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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