Recyclable thermophilic hybrid protein-inorganic nanoflowers for the hydrolysis of milk lactose
Thermostable β-galactosidase (TmLac) has been immobilized as hybrid inorganic-protein nanoflowers using salts of Cu2+, Mn2+, Zn2+, Co2+ and Ca2+ as the inorganic component. The incorporation efficiency of enzyme into the nanoflowers was higher than 95% for a protein concentration of 0.05 mg/mL. The...
| Autores: | , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2020 |
| País: | España |
| Institución: | Universidad Católica de Valencia San Vicente Mártir |
| Repositorio: | RIUCV. Repositorio de la Universidad Católica de Valencia San Vicente Mártir |
| Idioma: | inglés |
| OAI Identifier: | oai:riucv.ucv.es:20.500.12466/3778 |
| Acceso en línea: | http://hdl.handle.net/20.500.12466/3778 |
| Access Level: | acceso abierto |
| Palabra clave: | β-Galactosidase Enzyme immobilization Lactose intolerance Milk products 2302 Bioquímica 2302.90 Bioquímica de Alimentos |
| Sumario: | Thermostable β-galactosidase (TmLac) has been immobilized as hybrid inorganic-protein nanoflowers using salts of Cu2+, Mn2+, Zn2+, Co2+ and Ca2+ as the inorganic component. The incorporation efficiency of enzyme into the nanoflowers was higher than 95% for a protein concentration of 0.05 mg/mL. The structure, activity and recyclability of the nanoflowers with different chemical composition were analyzed. Ca2+, Mn2+ and Co2+ nanoflowers showed a level of lactase activity equivalent to their same content of free enzyme. Cu2+nanoflowers showed only marginal enzyme activity in agreement with the inhibitory effect of this cation on the enzyme. TmLac nanoflowers provide an efficient methodology for enzyme immobilization and recyclability. TmLac-Ca2+ nanoflowers presented the best properties for lactose hydrolysis both in buffered and in milk, and could be reused in five consecutive cycles. |
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