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Characterization of catalase-negative mutants of methylotrophic yeast Hansenula polymorpha
LR. Aminova, E. Kyslíková, O. Volfová, YA. Trotsenko,
Jazyk angličtina Země Česko
Typ dokumentu časopisecké články
PubMed
1823652
Knihovny.cz E-zdroje
- MeSH
- katalasa genetika MeSH
- mutace * MeSH
- Pichia enzymologie genetika růst a vývoj MeSH
- subcelulární frakce enzymologie metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
Three recently isolated catalase-negative mutants of Hansenula polymorpha lost the ability to grow on methanol but grew in media containing glucose, ethanol or glycerol. Their incubation in a medium with methanol resulted in an accumulation of hydrogen peroxide and cell death. During growth of a catalase-negative mutant in chemostat on a mixture of methanol and glucose, neither H2O2 accumulation nor cell death were observed up to the molar ratio of 10:1 of the two substrates. Cytochrome-c peroxidase and NADH-peroxidase activities were detected in the cells. In methylotrophic yeasts, catalase seems to be an enzyme characteristic of the metabolism of methanol but not needed for the metabolism of multicarbon substrates. The hydrogen peroxide produced during growth of the mutants on mixed substrates is detoxified by cytochrome-c peroxidase and other peroxidases.
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- $a Characterization of catalase-negative mutants of methylotrophic yeast Hansenula polymorpha / $c LR. Aminova, E. Kyslíková, O. Volfová, YA. Trotsenko,
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- $a Three recently isolated catalase-negative mutants of Hansenula polymorpha lost the ability to grow on methanol but grew in media containing glucose, ethanol or glycerol. Their incubation in a medium with methanol resulted in an accumulation of hydrogen peroxide and cell death. During growth of a catalase-negative mutant in chemostat on a mixture of methanol and glucose, neither H2O2 accumulation nor cell death were observed up to the molar ratio of 10:1 of the two substrates. Cytochrome-c peroxidase and NADH-peroxidase activities were detected in the cells. In methylotrophic yeasts, catalase seems to be an enzyme characteristic of the metabolism of methanol but not needed for the metabolism of multicarbon substrates. The hydrogen peroxide produced during growth of the mutants on mixed substrates is detoxified by cytochrome-c peroxidase and other peroxidases.
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