1. Alcohol oxidase of methylotrophic thermo- and acidotolerant yeast Hansenula sp
- Author
-
Bystrykh Lv, Dvoráková J, and O. Volfová
- Subjects
chemistry.chemical_classification ,Molar mass ,Chromatography ,biology ,Stereochemistry ,Macromolecular Substances ,General Medicine ,Hydrogen-Ion Concentration ,biology.organism_classification ,Microbiology ,Michaelis–Menten kinetics ,Pichia ,Pichia pastoris ,Alcohol oxidase ,Enzyme binding ,Alcohol Oxidoreductases ,Kinetics ,Enzyme ,chemistry ,Tetramer ,Saccharomycetales ,Protein quaternary structure ,Electrophoresis, Polyacrylamide Gel ,Chromatography, High Pressure Liquid - Abstract
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.
- Published
- 1989