Details
| Original language | English |
|---|---|
| Pages (from-to) | 3800-3812 |
| Number of pages | 13 |
| Journal | Applied Biochemistry and Biotechnology |
| Volume | 175 |
| Issue number | 8 |
| Publication status | Published - 19 Feb 2015 |
Abstract
A β-carotene-degrading enzyme activity was observed in liquid cultures of the basidiomycete Ganoderma applanatum. Supplementing the cultures with β-carotene induced the bleaching activity. Purification via hydrophobic interaction, ion exchange and size exclusion chromatography followed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) resulted in a single protein band. LC-ion-trap-MS analyses and gene amplification identified two manganese peroxidase isoenzymes with 97.8 % identity on the amino acid level. These showed an estimated molecular mass of 48 kDa and an isoelectric point of 2.6. Properties not yet described for other manganese peroxidases were hydrogen-peroxide-independent catalysis and two maxima of the bleaching activity, a distinct one at pH 5 and a lower one at pH 8. During simulated washing studies, the applicability of the isoenzymes for the brightening of carotenoids under alkaline conditions was proven. The new enzymes may replace common bleaching agents to produce environmentally more compatible detergent formulations.
Keywords
- Alkaline activity, Biocatalysis, Carotene degradation, Enzyme activity, Filamentous fungi, Ganoderma applanatum, Manganese peroxidase, Purification, Washing
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
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
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In: Applied Biochemistry and Biotechnology, Vol. 175, No. 8, 19.02.2015, p. 3800-3812.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Manganese Peroxidases from Ganoderma applanatum Degrade β-Carotene Under Alkaline Conditions
AU - Lanfermann, Isabel
AU - Linke, Diana
AU - Nimtz, Manfred
AU - Berger, Ralf G.
PY - 2015/2/19
Y1 - 2015/2/19
N2 - A β-carotene-degrading enzyme activity was observed in liquid cultures of the basidiomycete Ganoderma applanatum. Supplementing the cultures with β-carotene induced the bleaching activity. Purification via hydrophobic interaction, ion exchange and size exclusion chromatography followed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) resulted in a single protein band. LC-ion-trap-MS analyses and gene amplification identified two manganese peroxidase isoenzymes with 97.8 % identity on the amino acid level. These showed an estimated molecular mass of 48 kDa and an isoelectric point of 2.6. Properties not yet described for other manganese peroxidases were hydrogen-peroxide-independent catalysis and two maxima of the bleaching activity, a distinct one at pH 5 and a lower one at pH 8. During simulated washing studies, the applicability of the isoenzymes for the brightening of carotenoids under alkaline conditions was proven. The new enzymes may replace common bleaching agents to produce environmentally more compatible detergent formulations.
AB - A β-carotene-degrading enzyme activity was observed in liquid cultures of the basidiomycete Ganoderma applanatum. Supplementing the cultures with β-carotene induced the bleaching activity. Purification via hydrophobic interaction, ion exchange and size exclusion chromatography followed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) resulted in a single protein band. LC-ion-trap-MS analyses and gene amplification identified two manganese peroxidase isoenzymes with 97.8 % identity on the amino acid level. These showed an estimated molecular mass of 48 kDa and an isoelectric point of 2.6. Properties not yet described for other manganese peroxidases were hydrogen-peroxide-independent catalysis and two maxima of the bleaching activity, a distinct one at pH 5 and a lower one at pH 8. During simulated washing studies, the applicability of the isoenzymes for the brightening of carotenoids under alkaline conditions was proven. The new enzymes may replace common bleaching agents to produce environmentally more compatible detergent formulations.
KW - Alkaline activity
KW - Biocatalysis
KW - Carotene degradation
KW - Enzyme activity
KW - Filamentous fungi
KW - Ganoderma applanatum
KW - Manganese peroxidase
KW - Purification
KW - Washing
UR - http://www.scopus.com/inward/record.url?scp=84939976319&partnerID=8YFLogxK
U2 - 10.1007/s12010-015-1548-8
DO - 10.1007/s12010-015-1548-8
M3 - Article
C2 - 25690352
AN - SCOPUS:84939976319
VL - 175
SP - 3800
EP - 3812
JO - Applied Biochemistry and Biotechnology
JF - Applied Biochemistry and Biotechnology
SN - 0273-2289
IS - 8
ER -