Alcohol oxidase of methylotrophic thermo- and acidotolerant yeast Hansenula sp
Language English Country United States Media print
Document type Journal Article
PubMed
2680833
DOI
10.1007/bf02821297
Knihovny.cz E-resources
- MeSH
- Alcohol Oxidoreductases isolation & purification metabolism MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Kinetics MeSH
- Hydrogen-Ion Concentration MeSH
- Macromolecular Substances MeSH
- Pichia enzymology MeSH
- Saccharomycetales enzymology MeSH
- Chromatography, High Pressure Liquid MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Alcohol Oxidoreductases MeSH
- Macromolecular Substances MeSH
Electrophoretic analysis of alcohol oxidase purified from the methylotrophic thermo- and acidotolerant yeast Hansenula sp. revealed the presence of two active forms of the enzyme with molar mass 440 kg/mol (major component) and 724 kg/mol (minor component). A subunit M of the enzyme was found to be 72 kg/mol. Two active forms of the enzyme found by electrophoresis seem to be caused by dissociation of the octameric form to the tetramer under alkaline conditions. Studies of alcohol oxidase showed a kinetic variability of the enzyme with respect to its Km. It is proposed that the variability of Km is caused by enzyme binding to formaldehyde.
