Protective role of trehalose on thermal stability of lactase in relation to its glass and crystal forming properties and effect of delaying crystallization
Thermal inactivation of β-galactosidase was investigated in dried matrices of poly(vinyl)pyrrolidone (PVP), maltodextrin and trehalose. Significant lactase inactivation was observed in the polymeric matrices kept well below their glass transition temperature (Tg). The stability of the enzyme in the...
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| Autores principales: | , , |
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| Formato: | JOUR |
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00236438_v30_n3_p324_Mazzobre |
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| Sumario: | Thermal inactivation of β-galactosidase was investigated in dried matrices of poly(vinyl)pyrrolidone (PVP), maltodextrin and trehalose. Significant lactase inactivation was observed in the polymeric matrices kept well below their glass transition temperature (Tg). The stability of the enzyme in the anhydrous glassy matrices of maltodextrin and PVPs heated at 70 °C was directly related to their Tg; i.e. systems with higher glass transition temperature afforded better thermal protection of lactase. However, the stability of lactase in the heated trehalose matrix deviated from this behaviour since enzyme stability was higher than expected on the basis of the results obtained with polymeric matrices. In systems in which the trehalose matrix was rehumidified to conditions which allowed a high proportion of trehalose to crystallize, the enzyme was rapidly inactivated upon heating. Addition of maltodextrin to trehalose matrix provided enhanced protection to the enzyme, and this was probably due to delayed trehalose crystal formation. © 1997 Academic Press Limited. |
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