Stabilization studies of Fomes sclerodermeus laccases

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 th...

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Autores principales:	Papinutti, Víctor Leandro, Forchíassin, Flavia
Publicado:	2008
Materias:	Additives Fomes sclerodermeus Laccase Stability Inactivation pattern Aldehydes Glycerol pH effects Thermal effects Enzymes 1 hydroxybenzotriazole copper sulfate drug additive glutaraldehyde glycerol laccase mannitol trehalose unclassified drug veratryl alcohol electrokinesis enzyme activity pH temperature effect wheat article Basidiomycetes enzyme stability half life time nonhuman priority journal temperature wheat bran Basidiomycota Enzyme Stability Hydrogen-Ion Concentration Isoenzymes Kinetics Thermodynamics Triticum Fomes Triticum aestivum
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09608524_v99_n2_p419_Papinutti http://hdl.handle.net/20.500.12110/paper_09608524_v99_n2_p419_Papinutti
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_09608524_v99_n2_p419_Papinutti
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spelling	paper:paper_09608524_v99_n2_p419_Papinutti2023-06-08T15:57:47Z Stabilization studies of Fomes sclerodermeus laccases Papinutti, Víctor Leandro Forchíassin, Flavia 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 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. Fil:Papinutti, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Forchiassin, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2008 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09608524_v99_n2_p419_Papinutti http://hdl.handle.net/20.500.12110/paper_09608524_v99_n2_p419_Papinutti
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	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
spellingShingle	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 Papinutti, Víctor Leandro Forchíassin, Flavia Stabilization studies of Fomes sclerodermeus laccases
topic_facet	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
description	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.
author	Papinutti, Víctor Leandro Forchíassin, Flavia
author_facet	Papinutti, Víctor Leandro Forchíassin, Flavia
author_sort	Papinutti, Víctor Leandro
title	Stabilization studies of Fomes sclerodermeus laccases
title_short	Stabilization studies of Fomes sclerodermeus laccases
title_full	Stabilization studies of Fomes sclerodermeus laccases
title_fullStr	Stabilization studies of Fomes sclerodermeus laccases
title_full_unstemmed	Stabilization studies of Fomes sclerodermeus laccases
title_sort	stabilization studies of fomes sclerodermeus laccases
publishDate	2008
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09608524_v99_n2_p419_Papinutti http://hdl.handle.net/20.500.12110/paper_09608524_v99_n2_p419_Papinutti
work_keys_str_mv	AT papinuttivictorleandro stabilizationstudiesoffomessclerodermeuslaccases AT forchiassinflavia stabilizationstudiesoffomessclerodermeuslaccases
_version_	1768543620620615680

Stabilization studies of Fomes sclerodermeus laccases

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