title: Temperature affects the production, activity and stability of ligninolytic enzymes in Pleurotus ostreatus and Trametes versicolor.
abstract: Enzyme activity was determined in cultures of Pleurotus ostreatus and Trametes versicolor with cellulose as a sole C source and high C/N ratio. The fungi were able to grow and produce laccase and Mn-peroxidase (MnP) at 5-35 degrees C, the highest production being recorded at 25-30 degrees C in P. ostreatus and at 35 degrees C in T. versicolor. Production of both enzymes at 10 degrees C accounted only for 4-20% of the maximum value. Temperature optima for enzyme activity were 50 and 55 degrees C for P. ostreatus and T. versicolor laccases, respectively, and 60 degrees C for MnP. Temperatures causing 50% loss of activity after 24 h were 32 and 47 degrees C for laccases and 36 and 30 degrees C for MnP from P. ostreatus and T. versicolor, respectively.
authors.affiliation: Laboratory of Biochemistry of Wood-Rotting Fungi, Institute of Microbiology, Academy of Sciences of the Czech Republic, 142 20 Prague, Czechia.
authors.forename: J
authors.initials: J
authors.lastname: Snajdr
authors.forename: P
authors.initials: P
authors.lastname: Baldrian
mesh_terms: D004795:Enzyme Stability; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D042845:Laccase / Q000737:chemistry / Q000378:metabolism*; D008031:Lignin / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D020076:Pleurotus / Q000201:enzymology* / Q000254:growth & development; D020072:Polyporales / Q000201:enzymology* / Q000254:growth & development; D013696:Temperature
chemical_list: D005656:Fungal Proteins; D008031:Lignin; D042845:Laccase; D010544:Peroxidases; C051129:manganese peroxidase