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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todo:paper_09608524_v99_n2_p419_Papinutti2023-10-03T15:53:57Z Stabilization studies of Fomes sclerodermeus laccases Papinutti, L. Dimitriu, P. Forchiassin, F. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_09608524_v99_n2_p419_Papinutti |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
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R-134 |
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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, L. Dimitriu, P. Forchiassin, F. 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. |
| format |
JOUR |
| author |
Papinutti, L. Dimitriu, P. Forchiassin, F. |
| author_facet |
Papinutti, L. Dimitriu, P. Forchiassin, F. |
| author_sort |
Papinutti, L. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_09608524_v99_n2_p419_Papinutti |
| work_keys_str_mv |
AT papinuttil stabilizationstudiesoffomessclerodermeuslaccases AT dimitriup stabilizationstudiesoffomessclerodermeuslaccases AT forchiassinf stabilizationstudiesoffomessclerodermeuslaccases |
| _version_ |
1807315949334822912 |