Isolation and study of some properties of laccase from the basidiomycetes Cerrena maxima.
A new strain producing extracellular laccase (Cerrena maxima 0275) was found by screening of isolates of Basidiomycetes, and the dynamics of laccase biosynthesis by this strain was studied. The enzyme was purified to homogeneity. The molecular weight of the enzyme is 57 kD, and its pI is 3.5. The activity is constant at pH values in the range 3.0-5.0. The temperature optimum for activity is 50 degrees C. The thermal stability of the laccase was studied. The catalytic and Michaelis constants for catechol, hydroquinone, sinapinic acid, and K4Fe(CN)6 were determined. The standard redox potential of type 1 copper in the enzyme is 750 +/- 5 mV. Thus, the investigated laccase is a high redox potential laccase.
Koroleva
O V
OV
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 117071, Russia. alena_koroleva@hotmail.com
Yavmetdinov
I S
IS
Shleev
S V
SV
Stepanova
E V
EV
Gavrilova
V P
VP
D001487:Basidiomycota / Q000737:chemistry / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007700:Kinetics; D042845:Laccase; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D013696:Temperature
D010088:Oxidoreductases; D042845:Laccase