Página Inicial CNEA Laboratorio TANDAR Página Inicial TANDAR Historia del acelerador TANDAR Web interno Web mail
Inicio » Actividades I+D > Publicaciones 2008 > Structure/Function Relationships of Seve...
artículo con referato
"Structure/Function Relationships of Several Biopolymers as Related to Invertase Stability in Dehydrated Systems"
P.R. Santagapita, L. Gómez Brizuela, M.F. Mazzobre, H.L. Ramirez, H.R. Corti, R. Villalonga Santana and M.P. Buera
Biomacromolecules 9(2) (2008) 741-747
Structure/function relationships of different biopolymers (alginate, dextran, or β-cyclodextrin) were analyzed as single excipients or combined with trehalose in relation to their efficiency as enzyme stabilizers in freeze-dried formulations and compared to trehalose. Particularly, a novel synthesized polymer β-cyclodextrin-branched alginate (β-CD-A) was employed as excipient. During freeze-drying, the polymers or their mixtures did not confer better protection to invertase compared to trehalose. β-CD-A (with or without trehalose), β-cyclodextrin (β-CD), or dextran with trehalose were the best protective agents during thermal treatment, while β-CD and alginate showed a negative effect on invertase activity preservation. The β-CD linked alginate combined the physical stability provided by alginate with the stabilization of hydrophobic regions of the enzyme provided by cyclodextrin. β-CD-A was effective even at conditions at which trehalose lost its protective effect. A relatively simple covalent combination of two biopolymers significantly affected their functionalities and, consequently, their interactions with proteins, modifying enzyme stability patterns.
Av. Gral Paz y Constituyentes, San Martín, Pcia. de Buenos Aires, Argentina
Tel: (54-11) 6772-7007 - Fax: (54-11) 6772-7121