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Characterization of an aryl-alcohol oxidase from the plant saprophytic basidiomycete Coprinopsis cinerea with broad substrate specificity against aromatic alcohols.
- Source :
-
Biotechnology letters [Biotechnol Lett] 2018 Jul; Vol. 40 (7), pp. 1077-1086. Date of Electronic Publication: 2018 May 22. - Publication Year :
- 2018
-
Abstract
- Objectives: The aim of the study was to obtain information about the enzymatic properties of aryl-alcohol oxidase from the plant saprophytic basidiomycete Coprinopsis cinerea (rCcAAO), which is classified into the auxiliary activities family 3 subfamily 2 (AA3&#95;2).<br />Results: The gene encoding AAO from the plant saprophytic basidiomycete Coprinopsis cinerea (CcAAO) was cloned, and the recombinant CcAAO (rCcAAO) was heterologously expressed in the methylotrophic yeast Pichia pastoris. The purified rCcAAO showed significant activity not only against trans,trans-2,4-hexadien-1-ol but also against a broad range of aromatic alcohols including aromatic compounds that were reported to be poor substrates for known AAOs. Moreover, site-directed mutagenesis analysis demonstrated that mutants with substitutions from leucine to phenylalanine and tryptophan at position 416 exhibited decreases of activity for aromatic alcohols but still maintained the activity for trans,trans-2,4-hexadien-1-ol.<br />Conclusions: Leucine 416 in CcAAO contributes to the broad substrate specificity against various aromatic alcohols, which is useful for the production of hydrogen peroxide using this enzyme.
- Subjects :
- Alcohols metabolism
Biodegradation, Environmental
Biomass
Cloning, Molecular
Escherichia coli genetics
Kinetics
Plants
Substrate Specificity
Agaricales enzymology
Agaricales genetics
Alcohol Oxidoreductases chemistry
Alcohol Oxidoreductases genetics
Alcohol Oxidoreductases metabolism
Fungal Proteins chemistry
Fungal Proteins genetics
Fungal Proteins metabolism
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1573-6776
- Volume :
- 40
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Biotechnology letters
- Publication Type :
- Academic Journal
- Accession number :
- 29785669
- Full Text :
- https://doi.org/10.1007/s10529-018-2534-3