Gums induced microstructure stability in Ca(II)-alginate beads containing lactase analyzed by SAXS
[EN] Previous works show that the addition of trehalose and gums in ß-galactosidase (lactase) Ca(II)-alginate encapsulation systems improved its intrinsic stability against freezing and dehydration processes in the pristine state. However, there is no available information on the evolution in micros...
| Autores: | , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2018 |
| País: | España |
| Institución: | Universitat Politècnica de València (UPV) |
| Repositorio: | RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia |
| Idioma: | inglés |
| OAI Identifier: | oai:riunet.upv.es:10251/141969 |
| Acceso en línea: | https://riunet.upv.es/handle/10251/141969 |
| Access Level: | acceso abierto |
| Palabra clave: | Alginate beads Hydrocolloids Encapsulation Beta-Galactosidase Microstructure Small-Angle X-ray scattering (SAXS) TECNOLOGIA DE ALIMENTOS |
| Sumario: | [EN] Previous works show that the addition of trehalose and gums in ß-galactosidase (lactase) Ca(II)-alginate encapsulation systems improved its intrinsic stability against freezing and dehydration processes in the pristine state. However, there is no available information on the evolution in microstructure due to the constraints imposed by the operational conditions. The aim of this research is to study the time course of microstructural changes of Ca(II)-alginate matrices driven by the presence of trehalose, arabic and guar gums as excipients and to discuss how these changes in¿uence the di¿usional transport (assessed by LF-NMR) and the enzymatic activity of the encapsulated lactase. The structural modi¿cations at di¿erent scales were assessed by SAXS. The incorporation of gums as second excipients induces a signi¿cant stabilization in the microstructure not only at the rod scale, but also in the characteristic size and density of alginate dimers (basic units of construction of rods) and the degree of interconnection of rods at a larger scale, improving the performance in terms of lactase activity. |
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