Food-grade Pickering stabilizers obtained from a protein-rich lupin cultivar (AluProt-CGNA®): Chemical characterization and emulsifying properties
Pickering stabilizers exhibit unique interfacial properties; however, only limited types of these particles are available for the food industry. Therefore, the main aim of this study was to develop a food-grade Pickering stabilizer using a protein isolate obtained from the protein-rich lupin variety...
| Autores: | , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión aceptada para publicación |
| Fecha de publicación: | 2019 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/200864 |
| Acceso en línea: | http://hdl.handle.net/10261/200864 |
| Access Level: | acceso abierto |
| Palabra clave: | AluProt-CGNA® Emulsifying properties Lupin protein isolate Pickering emulsions Pickering stabilizers Protein-rich |
| Sumario: | Pickering stabilizers exhibit unique interfacial properties; however, only limited types of these particles are available for the food industry. Therefore, the main aim of this study was to develop a food-grade Pickering stabilizer using a protein isolate obtained from the protein-rich lupin variety AluProt-CGNA® (LPIA). Lupin protein aggregate particles (LP-APs), obtained from LPIA, were produced through a facile and scalable technology based on heat-induced particle formation. LP-APs with high surface charge and partial wettability were effective for stabilizing O/W emulsions. These emulsions were prepared by using high-speed homogenization with LP-APs dispersions. The creaming index, microstructure and physicochemical properties of Pickering emulsions were investigated. The results showed that LP-APs exhibit great potential to perform as stabilizers for O/W Pickering emulsions (O/W). Additionally, LP-APs exhibited much better interfacial and emulsifying properties than did the unheated LPIA. Heating greatly improved the emulsification performance of protein particles, especially at high concentrations (>3%, w/v). The formed emulsions were highly stable against creaming upon storage over 14 days. These findings are of great importance for the formulation of LP-APs-based emulsions with improved properties (e.g., stable against creaming and coalescence) and will also significantly extend the application of lupin proteins in the food industry. © 2018 Elsevier Ltd |
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