Thermally stable and hydrogen peroxide tolerant manganese peroxidase (MnP) from Lenzites betulinus.
A thermally stable and hydrogen peroxide tolerant manganese peroxidase (MnP) was purified from the culture medium of Lenzites betulinus by ion exchange chromatography, gel filtration and isoelectric focusing chromatography. The MnP purified from L. betulinus (L-MnP) has a molecular mass of 40 kDa and its isoelectric point was determined to be 6.2. The first 19 amino acids at the N-terminal end of the L-MnP sequence were found to exhibit 74% identity with those of a Phlebia radiata MnP. L-MnP was proved to have the highest hydrogen peroxide tolerance among MnPs reported so far. It retained more than 60% of the initial activity after thermal treatment at 60 degrees C for 60 min, and also retained more than 60% of the initial activity after exposure to 10 mM hydrogen peroxide for 5 min at 37 degrees C.
Hoshino
Fumihiko
F
Toyota Central R&D Labs Inc., 41-1, Yokomichi, Nagakute, Aichi 480-1192, Japan.
Kajino
Tsutomu
T
Sugiyama
Hidehiko
H
Asami
Osamu
O
Takahashi
Haruo
H
D000363:Agaricales / Q000201:enzymology*; D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006861:Hydrogen Peroxide / Q000494:pharmacology*; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D006861:Hydrogen Peroxide; D010544:Peroxidases; C051129:manganese peroxidase