Temperature affects the production, activity and stability of ligninolytic enzymes in Pleurotus ostreatus and Trametes versicolor.
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.
Snajdr
J
J
Laboratory of Biochemistry of Wood-Rotting Fungi, Institute of Microbiology, Academy of Sciences of the Czech Republic, 142 20 Prague, Czechia.
Baldrian
P
P
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
D005656:Fungal Proteins; D008031:Lignin; D042845:Laccase; D010544:Peroxidases; C051129:manganese peroxidase