Use of a mixer-type rheometer for predicting the stability of O/W protein-based emulsions
The present work illustrates the feasibility of performing Oil-in-Water (O/W) emulsions stabilized by different protein concentrates, as well as predicting the likelihood of emulsion destabilization over ageing time just after its preparation. To achieve this objective, four protein sources (rice, c...
| Autores: | , , , , |
|---|---|
| Formato: | artículo |
| Estado: | Versión aceptada para publicación |
| Fecha de publicación: | 2017 |
| País: | España |
| Recursos: | Universidad de Sevilla (US) |
| Repositorio: | idUS. Depósito de Investigación de la Universidad de Sevilla |
| OAI Identifier: | oai:idus.us.es:11441/172457 |
| Acesso em linha: | https://hdl.handle.net/11441/172457 https://doi.org/10.1016/j.lwt.2017.07.008 |
| Access Level: | acceso abierto |
| Palavra-chave: | Mixer type rheometer Droplet size distribution Emulsification Proteins Viscosity |
| Resumo: | The present work illustrates the feasibility of performing Oil-in-Water (O/W) emulsions stabilized by different protein concentrates, as well as predicting the likelihood of emulsion destabilization over ageing time just after its preparation. To achieve this objective, four protein sources (rice, crayfish, potato and albumen) and four oil concentrations (450, 550, 650 and 750 g kg⁻¹) were used. The emulsification process was monitored by the use of a mixer-type rheometer. This rheometer was a valuable tool for understanding and controlling the emulsification process through the measurement of the viscosity of the different systems during the emulsification stage. Results reveal the importance of controlling the emulsification process to optimize the properties of the final emulsion, which is highly influenced by the oil concentration. Then, emulsions were characterized by means of flow properties and droplet size distribution (DSD). Eventually, a relationship was found that relates the rheological properties and the microstructure of the final emulsions during and after emulsification stage. These measurements have been demonstrated to be useful in order to predict the stability of protein-based emulsions. |
|---|