A peroxidase from Lepista irina cleaves β,β-carotene to flavor compounds

Research output: Contribution to journalArticleResearchpeer review

Authors

  • Holger Zorn
  • Sabine Langhoff
  • Manuela Scheibner
  • Manfred Nimtz
  • Ralf G. Berger

Research Organisations

External Research Organisations

  • Helmholtz Centre for Infection Research (HZI)
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Details

Original languageEnglish
Pages (from-to)1049-1056
Number of pages8
JournalBiological chemistry
Volume384
Issue number7
Publication statusPublished - 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

Cite this

A peroxidase from Lepista irina cleaves β,β-carotene to flavor compounds. / Zorn, Holger; Langhoff, Sabine; Scheibner, Manuela et al.
In: Biological chemistry, Vol. 384, No. 7, 01.07.2003, p. 1049-1056.

Research output: Contribution to journalArticleResearchpeer review

Zorn, H, Langhoff, S, Scheibner, M, Nimtz, M & Berger, RG 2003, 'A peroxidase from Lepista irina cleaves β,β-carotene to flavor compounds', Biological chemistry, vol. 384, no. 7, pp. 1049-1056. https://doi.org/10.1515/BC.2003.117
Zorn, H., Langhoff, S., Scheibner, M., Nimtz, M., & Berger, R. G. (2003). A peroxidase from Lepista irina cleaves β,β-carotene to flavor compounds. Biological chemistry, 384(7), 1049-1056. https://doi.org/10.1515/BC.2003.117
Zorn H, Langhoff S, Scheibner M, Nimtz M, Berger RG. A peroxidase from Lepista irina cleaves β,β-carotene to flavor compounds. Biological chemistry. 2003 Jul 1;384(7):1049-1056. doi: 10.1515/BC.2003.117
Zorn, Holger ; Langhoff, Sabine ; Scheibner, Manuela et al. / A peroxidase from Lepista irina cleaves β,β-carotene to flavor compounds. In: Biological chemistry. 2003 ; Vol. 384, No. 7. pp. 1049-1056.
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