Oxidation of methanol, formaldehyde and formate by catalase purified from methanol-grown Hansenula polymorpha.

Archives of microbiology ·Vol. 106 ·No. 3 ·1975-12-31 ·Pages 221-6

van Dijken JP, Otto R, Harder W

Abstract

Catalase has been partially purified from cell-free extracts of methanol-grown Hansenula polymorpha and its peroxidative properties were studied. It was shown that the enzyme is capable of oxidizing methanol, formaldehyde and formate in the presence of hydrogen peroxide. The physiological significance of these reactions in the transduction of energy from the oxidation of methanol in yeasts is discussed.

MeSH Terms

Ascomycota/enzymology Catalase/isolation & purification,metabolism Formaldehyde/metabolism Formates/metabolism Hydrogen Peroxide/metabolism Methanol/metabolism Pichia/enzymology

Chemicals

Formates Formaldehyde Hydrogen Peroxide Catalase Methanol

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

van Dijken J P

Otto R

Harder W

References (15)

15 references, click to expand

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Article Info

Journal

Archives of microbiology

Abbr.

Arch Microbiol

ISSN

0302-8933

DOI

10.1007/BF00446527

Published

1975-12-31

Pages

221-6

Language

English

Region

Germany

NLM ID

0410427

Subset

External Links

PubMed source DOI: 10.1007/BF00446527 View journal details

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Oxidation of methanol, formaldehyde and formate by catalase purified from methanol-grown Hansenula polymorpha.

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