Details
| Original language | English |
|---|---|
| Pages (from-to) | 1049-1056 |
| Number of pages | 8 |
| Journal | Biological chemistry |
| Volume | 384 |
| Issue number | 7 |
| Publication status | Published - 1 Jul 2003 |
Abstract
Extracellular liquid of the edible fungus Lepista irina was found to effectively degrade β,β-carotene. β-Ionone, β-cyclocitral, dihydroactinidiolide, and 2-hydroxy-2,6,6-trimethylcyclohexanone were formed as volatile breakdown products of β,β-carotene with mycelium-free culture supernatants, whereas β-apo-10′-carotenal was identified as non-volatile degradation product. The key enzyme catalyzing the oxidative cleavage of β,β-carotene was purified with an overall yield of 63% and a purification factor of 43. Biochemical characterization showed a molecular mass of 50.5 kDa and an isoelectric point of 3.75. Fastest β,β-carotene degradation occurred at 34 °C and pH values between 3.5 and 4. Degenerate oligonucleotides were derived from N-terminal and internal amino acid sequences. By means of PCR-based cDNA-library screening a 1284 bp cDNA was identified which showed great overall similarity to Pleurotus eryngii polyvalent peroxidases. The obtained sequence contains an open reading frame of 1083 nucleotides, encoding a polypeptide of 361 amino acids. A 30 amino acid signal peptide was identified upstream of the N-terminal sequence of the mature enzyme. The L. irina versatile peroxidase represents the first microbial enzyme capable of carotenoid degradation that has been characterized on a molecular level, proving the participation of extracellular enzymes of white rot fungi in biotic carotenoid degradation processes.
Keywords
- Basidiomycete, cDNA, Cleavage, Degradation, Norisoprenoids
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Clinical Biochemistry
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In: Biological chemistry, Vol. 384, No. 7, 01.07.2003, p. 1049-1056.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - A peroxidase from Lepista irina cleaves β,β-carotene to flavor compounds
AU - Zorn, Holger
AU - Langhoff, Sabine
AU - Scheibner, Manuela
AU - Nimtz, Manfred
AU - Berger, Ralf G.
PY - 2003/7/1
Y1 - 2003/7/1
N2 - Extracellular liquid of the edible fungus Lepista irina was found to effectively degrade β,β-carotene. β-Ionone, β-cyclocitral, dihydroactinidiolide, and 2-hydroxy-2,6,6-trimethylcyclohexanone were formed as volatile breakdown products of β,β-carotene with mycelium-free culture supernatants, whereas β-apo-10′-carotenal was identified as non-volatile degradation product. The key enzyme catalyzing the oxidative cleavage of β,β-carotene was purified with an overall yield of 63% and a purification factor of 43. Biochemical characterization showed a molecular mass of 50.5 kDa and an isoelectric point of 3.75. Fastest β,β-carotene degradation occurred at 34 °C and pH values between 3.5 and 4. Degenerate oligonucleotides were derived from N-terminal and internal amino acid sequences. By means of PCR-based cDNA-library screening a 1284 bp cDNA was identified which showed great overall similarity to Pleurotus eryngii polyvalent peroxidases. The obtained sequence contains an open reading frame of 1083 nucleotides, encoding a polypeptide of 361 amino acids. A 30 amino acid signal peptide was identified upstream of the N-terminal sequence of the mature enzyme. The L. irina versatile peroxidase represents the first microbial enzyme capable of carotenoid degradation that has been characterized on a molecular level, proving the participation of extracellular enzymes of white rot fungi in biotic carotenoid degradation processes.
AB - Extracellular liquid of the edible fungus Lepista irina was found to effectively degrade β,β-carotene. β-Ionone, β-cyclocitral, dihydroactinidiolide, and 2-hydroxy-2,6,6-trimethylcyclohexanone were formed as volatile breakdown products of β,β-carotene with mycelium-free culture supernatants, whereas β-apo-10′-carotenal was identified as non-volatile degradation product. The key enzyme catalyzing the oxidative cleavage of β,β-carotene was purified with an overall yield of 63% and a purification factor of 43. Biochemical characterization showed a molecular mass of 50.5 kDa and an isoelectric point of 3.75. Fastest β,β-carotene degradation occurred at 34 °C and pH values between 3.5 and 4. Degenerate oligonucleotides were derived from N-terminal and internal amino acid sequences. By means of PCR-based cDNA-library screening a 1284 bp cDNA was identified which showed great overall similarity to Pleurotus eryngii polyvalent peroxidases. The obtained sequence contains an open reading frame of 1083 nucleotides, encoding a polypeptide of 361 amino acids. A 30 amino acid signal peptide was identified upstream of the N-terminal sequence of the mature enzyme. The L. irina versatile peroxidase represents the first microbial enzyme capable of carotenoid degradation that has been characterized on a molecular level, proving the participation of extracellular enzymes of white rot fungi in biotic carotenoid degradation processes.
KW - Basidiomycete
KW - cDNA
KW - Cleavage
KW - Degradation
KW - Norisoprenoids
UR - http://www.scopus.com/inward/record.url?scp=0042856235&partnerID=8YFLogxK
U2 - 10.1515/BC.2003.117
DO - 10.1515/BC.2003.117
M3 - Article
C2 - 12956421
AN - SCOPUS:0042856235
VL - 384
SP - 1049
EP - 1056
JO - Biological chemistry
JF - Biological chemistry
SN - 1431-6730
IS - 7
ER -