IQUIBICEN   23947
INSTITUTO DE QUIMICA BIOLOGICA DE LA FACULTAD DE CIENCIAS EXACTAS Y NATURALES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Analysis of the Functional and Structural Stability of Beta-Glucosidase BglA from Cytophaga hutchinsonii.
Autor/es:
IGLESIAS RANDO M.; CRAIG PO.; GOROJOVSKY N.; GOLDBAUM FA.
Lugar:
La Plata
Reunión:
Congreso; Reunión Anual de la Sociedad Argentina de Biofísica 2018; 2018
Institución organizadora:
Sociedad Argentina de Biofísica
Resumen:
Cytophaga hutchinsonii is a gram-negative bacterium that can efficiently degrade crystalline cellulose through a combination of different cellulases. The enzymes involved in this process are potentially useful for biofuel production. BglA is a beta-glucosidase from this bacterium which produces the hydrolysis of cellobiose into glucose. The cloning and recombinant expression of this enzyme in E. coli yields large amounts of soluble protein. It has a good activity and a low inhibition rate by glucose which makes it attractive for industrial purposes. However, it is somewhat sensitive to temperature. Here we present an analysis of the temperature dependence of the enzyme activity and its inactivation rate. The activity is optimal around 25°C but sharply decays above 30°C in an irreversible process. To evaluate the possibility of inactivation by the oxidation of catalytic important residues we studied how BglA's activity loss was affected in reducing conditions in the presence of DTT. We also present an analysis of the urea induced denaturation of this multidomain protein followed by intrinsic tryptophan fluorescence, ANS binding, CD signal and enzymatic activity. Perspectives for the thermal stabilization of this enzyme and its possible use in synthetic multienzymatic complexes (artificial cellulosomes) for improving lignocellulose degradation is discussed.p { margin-bottom: 0.1in; direction: ltr; color: rgb(0, 0, 10); line-height: 120%; text-align: left; background: transparent none repeat scroll 0% 0%; }p.western { font-family: "Calibri", serif; font-size: 11pt; }p.cjk { font-family: "Calibri"; font-size: 11pt; }p.ctl { font-size: 11pt; }