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Abstract:

Stability of laccase isoenzymes from a crude extract obtained from Fomes sclerodermeus grown on wheat bran medium was studied. The variables assessed were temperature, pH and additives. As revealed by PAGE, three bands of laccase, each with different thermal inactivation pattern, were detected in the crude extract: after 6 h at 50 °C and pH 8, Lc2 was the most resistant, while the Lc1 and Lc3 bands were almost completely inactivated. This pattern of inactivation was observed at all temperatures and pH tested. Laccase activity was more stable in the 5-10 pH range when incubated at 40 and 50 °C; at 30 °C and 24 h the enzyme remained fully active in the 3-11 pH range. The effect of additives (veratryl alcohol, trehalose, glycerol, mannitol, glutaraldehyde, CuSO4 and 1-HBT) on laccase stability was tested. The stability was enhanced with CuSO4 (1.25 mM), glycerol (0.2%) and mannitol (1%). The presence of both CuSO4 and glycerol caused a 3-fold increase in the half-life values. © 2007 Elsevier Ltd. All rights reserved.

Registro:

Documento: Artículo
Título:Stabilization studies of Fomes sclerodermeus laccases
Autor:Papinutti, L.; Dimitriu, P.; Forchiassin, F.
Filiación:Laboratorio de Micología Experimental, Departamento de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, 1428 Buenos Aires, Argentina
Palabras clave:Additives; Fomes sclerodermeus; Laccase; Stability; Fomes sclerodermeus; Inactivation pattern; Laccase; Additives; Aldehydes; Glycerol; pH effects; Thermal effects; Enzymes; 1 hydroxybenzotriazole; copper sulfate; drug additive; glutaraldehyde; glycerol; laccase; mannitol; trehalose; unclassified drug; veratryl alcohol; Additives; Aldehydes; Enzymes; Glycerol; pH effects; Thermal effects; electrokinesis; enzyme activity; pH; temperature effect; wheat; article; Basidiomycetes; enzyme stability; Fomes sclerodermeus; half life time; nonhuman; pH; priority journal; temperature; wheat bran; Basidiomycota; Enzyme Stability; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Laccase; Thermodynamics; Triticum; Fomes; Triticum aestivum
Año:2008
Volumen:99
Número:2
Página de inicio:419
Página de fin:424
DOI: http://dx.doi.org/10.1016/j.biortech.2006.11.061
Título revista:Bioresource Technology
Título revista abreviado:Bioresour. Technol.
ISSN:09608524
CODEN:BIRTE
CAS:1 hydroxybenzotriazole, 2592-95-2; copper sulfate, 7758-98-7, 7758-99-8; glutaraldehyde, 111-30-8, 37245-61-7; glycerol, 56-81-5; laccase, 80498-15-3; mannitol, 69-65-8, 87-78-5; trehalose, 99-20-7; veratryl alcohol, 93-03-8; Isoenzymes; Laccase, 1.10.3.2
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09608524_v99_n2_p419_Papinutti

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Citas:

---------- APA ----------
Papinutti, L., Dimitriu, P. & Forchiassin, F. (2008) . Stabilization studies of Fomes sclerodermeus laccases. Bioresource Technology, 99(2), 419-424.
http://dx.doi.org/10.1016/j.biortech.2006.11.061
---------- CHICAGO ----------
Papinutti, L., Dimitriu, P., Forchiassin, F. "Stabilization studies of Fomes sclerodermeus laccases" . Bioresource Technology 99, no. 2 (2008) : 419-424.
http://dx.doi.org/10.1016/j.biortech.2006.11.061
---------- MLA ----------
Papinutti, L., Dimitriu, P., Forchiassin, F. "Stabilization studies of Fomes sclerodermeus laccases" . Bioresource Technology, vol. 99, no. 2, 2008, pp. 419-424.
http://dx.doi.org/10.1016/j.biortech.2006.11.061
---------- VANCOUVER ----------
Papinutti, L., Dimitriu, P., Forchiassin, F. Stabilization studies of Fomes sclerodermeus laccases. Bioresour. Technol. 2008;99(2):419-424.
http://dx.doi.org/10.1016/j.biortech.2006.11.061