Interfacial and (emulsion) gel rheology of hydrophobised whey proteins
| Autor: | Ashkan Madadlou, Didier Dupont, Florence Rousseau, Juliane Floury, Marie-Hélène Famelart, Stéphane Pezennec |
|---|---|
| Přispěvatelé: | Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro) |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
gel
émulsion gouttelette whey paste Erythritol Flow stress Applied Microbiology and Biotechnology Viscoelasticity chemistry.chemical_compound 0404 agricultural biotechnology protéine de lait Rheology [SDV.IDA]Life Sciences [q-bio]/Food engineering alginate rhéologie Heat denaturation hydrophobicity emulsion lactoserum lactosérum 0402 animal and dairy science rhéologie interfaciale 04 agricultural and veterinary sciences Dynamic mechanical analysis 040401 food science 040201 dairy & animal science hydrophobicité chemistry Chemical engineering hydrophobisation Emulsion droplet rheology Dispersion (chemistry) erythritol [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition Food Science |
| Zdroj: | International Dairy Journal International Dairy Journal, Elsevier, 2020, 100, pp.104556. ⟨10.1016/j.idairyj.2019.104556⟩ |
| ISSN: | 0958-6946 |
| Popis: | Hydrophobisation of whey proteins, followed by erythritol addition into the hydrophobised protein dispersion, enables formation of water-in-water (W/W) emulsions of the proteins and alginate. In this study, we investigated the interfacial and gel rheology of whey proteins as affected by hydrophobisation, heat denaturation and erythritol addition. Additionally, the gel rheology of the resultant W/W emulsion was assessed. Hydrophobisation shortened the linear viscoelastic region and decreased the surface storage modulus ( G s ' ), the flow stress and the flow strain of protein layer at the air-liquid interface. Erythritol addition into the hydrophobised protein caused a further reduction of G s ' . In accordance with interfacial rheology, protein hydrophobisation and erythritol addition decreased the dynamic moduli of acid-induced protein gels. Frequency sweep tests indicated that the gelled emulsion had higher dynamic moduli than all WPI gels. The higher firmness of the emulsion gel was ascribed, based on microstructural images, to micro-phase separation of alginate droplets. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect