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Alcohol oxidase of methylotrophic thermo- and acidotolerant yeast Hansenula sp.

Authors
  • Bystrykh, L V
  • Dvoráková, J
  • Volfová, O
Type
Published Article
Journal
Folia microbiologica
Publication Date
Jan 01, 1989
Volume
34
Issue
3
Pages
233–237
Identifiers
PMID: 2680833
Source
Medline
License
Unknown

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.

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