Details
| Original language | English |
|---|---|
| Pages (from-to) | 7-12 |
| Number of pages | 6 |
| Journal | Enzyme and microbial technology |
| Volume | 61-62 |
| Publication status | Published - 23 Apr 2014 |
Abstract
An intracellular alcohol oxidase (AOX) was isolated from the white-rot basidiomycete Phanerochaete chrysosporium (Pch), grown on l-lactate induction medium, and purified to electrophoretic homogeneity. The dimeric protein consisted of two identical 75. kDa subunits. The open reading frame of 1,956. bp resulted in a monomer consisting of 651 amino acids. The enzyme showed a p. I at 5.4, a pH optimum of 9, a temperature optimum at 50. °C, possessed putative conserved domains of the GMC superfamily, a FAD binding domain, and showed up to 86% homology to alcohol oxidase sequences of Gloeophyllum trabeum and Coprinopsis cinerea. As was shown for the first time for an AOX from a basidiomycete, not only methanol, but also lower primary alcohols and glycerol were accepted as substrates. An assay based on aldehyde dehydrogenase confirmed d-glyceraldehyde as the product of the reaction. A bioprocess based on this enzyme could alleviate the problems associated with the huge side-stream of glycerol occurring during the manufacture of biodiesel, yielding the green oxidant hydrogen peroxide.
Keywords
- Alcohol oxidase, Glycerol, Phanerochaete chrysosporium
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Chemical Engineering(all)
- Bioengineering
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
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In: Enzyme and microbial technology, Vol. 61-62, 23.04.2014, p. 7-12.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - An alcohol oxidase of Phanerochaete chrysosporium with a distinct glycerol oxidase activity
AU - Linke, Diana
AU - Lehnert, Nicole
AU - Nimtz, Manfred
AU - Berger, Ralf G.
PY - 2014/4/23
Y1 - 2014/4/23
N2 - An intracellular alcohol oxidase (AOX) was isolated from the white-rot basidiomycete Phanerochaete chrysosporium (Pch), grown on l-lactate induction medium, and purified to electrophoretic homogeneity. The dimeric protein consisted of two identical 75. kDa subunits. The open reading frame of 1,956. bp resulted in a monomer consisting of 651 amino acids. The enzyme showed a p. I at 5.4, a pH optimum of 9, a temperature optimum at 50. °C, possessed putative conserved domains of the GMC superfamily, a FAD binding domain, and showed up to 86% homology to alcohol oxidase sequences of Gloeophyllum trabeum and Coprinopsis cinerea. As was shown for the first time for an AOX from a basidiomycete, not only methanol, but also lower primary alcohols and glycerol were accepted as substrates. An assay based on aldehyde dehydrogenase confirmed d-glyceraldehyde as the product of the reaction. A bioprocess based on this enzyme could alleviate the problems associated with the huge side-stream of glycerol occurring during the manufacture of biodiesel, yielding the green oxidant hydrogen peroxide.
AB - An intracellular alcohol oxidase (AOX) was isolated from the white-rot basidiomycete Phanerochaete chrysosporium (Pch), grown on l-lactate induction medium, and purified to electrophoretic homogeneity. The dimeric protein consisted of two identical 75. kDa subunits. The open reading frame of 1,956. bp resulted in a monomer consisting of 651 amino acids. The enzyme showed a p. I at 5.4, a pH optimum of 9, a temperature optimum at 50. °C, possessed putative conserved domains of the GMC superfamily, a FAD binding domain, and showed up to 86% homology to alcohol oxidase sequences of Gloeophyllum trabeum and Coprinopsis cinerea. As was shown for the first time for an AOX from a basidiomycete, not only methanol, but also lower primary alcohols and glycerol were accepted as substrates. An assay based on aldehyde dehydrogenase confirmed d-glyceraldehyde as the product of the reaction. A bioprocess based on this enzyme could alleviate the problems associated with the huge side-stream of glycerol occurring during the manufacture of biodiesel, yielding the green oxidant hydrogen peroxide.
KW - Alcohol oxidase
KW - Glycerol
KW - Phanerochaete chrysosporium
UR - http://www.scopus.com/inward/record.url?scp=84900462279&partnerID=8YFLogxK
U2 - 10.1016/j.enzmictec.2014.04.001
DO - 10.1016/j.enzmictec.2014.04.001
M3 - Article
C2 - 24910330
AN - SCOPUS:84900462279
VL - 61-62
SP - 7
EP - 12
JO - Enzyme and microbial technology
JF - Enzyme and microbial technology
SN - 0141-0229
ER -