Thermally stable and hydrogen peroxide tolerant manganese peroxidase (MnP) fromLenzites betulinus
| Autor: | Fumihiko Hoshino, Hidehiko Sugiyama, Haruo Takahashi, Tsutomu Kajino, Osamu Asami |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Molecular Sequence Data
Size-exclusion chromatography ved/biology.organism_classification_rank.species Ion chromatography Biophysics Biochemistry Phlebia radiata chemistry.chemical_compound Structural Biology Manganese peroxidase Enzyme Stability Genetics Amino Acid Sequence Hydrogen peroxide Molecular Biology Chromatography Sequence Homology Amino Acid Ion exchange Chemistry Isoelectric focusing ved/biology Thermal stability Cell Biology Chromatography Ion Exchange Isoelectric point Peroxidases Electrophoresis Polyacrylamide Gel Agaricales |
| Zdroj: | FEBS Letters. 530:249-252 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(02)03454-3 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text