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

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dc.identifier.uri http://dx.doi.org/10.15488/239
dc.identifier.uri http://www.repo.uni-hannover.de/handle/123456789/261
dc.contributor.author Zorn, Holger
dc.contributor.author Langhoff, Sabine
dc.contributor.author Scheibner, Manuela
dc.contributor.author Nimtz, Manfred
dc.contributor.author Berger, Ralf Günter
dc.date.accessioned 2016-03-04T11:42:38Z
dc.date.available 2016-03-04T11:42:38Z
dc.date.issued 2003-07
dc.identifier.citation Zorn, Holger; Langhoff, S.; Scheibner, M.; Nimtz, M.; Berger, R. G.: A peroxidase from Lepista irina cleaves beta,beta-carotene to flavor compounds. In: Biological Chemistry 384 (2003), Nr. 7, S. 1049-1056. DOI: http://dx.doi.org/10.1515/BC.2003.117
dc.description.abstract Extracellular liquid of the edible fungus Lepista irina was found to effectively degrade beta,beta-carotene. beta-Ionone, beta-cyclocitral, dihydroactinidiolide, and 2-hydroxy-2,6,6-trimethylcyclohexanone were formed as volatile breakdown products of beta,beta-carotene with myceliumfree culture supernatants, whereas beta-apo 10'-carotenal was identified as nonvolatile degradation product. The key enzyme catalyzing the oxidative cleavage of beta,beta-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 beta,beta carotene degradation occurred at 34degreesC and pH values between 3.5 and 4. Degenerate oligonucleotides were derived from Nterminal and internal amino acid sequences. By means of PCRbased cDNAlibrary 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 Nterminal 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. eng
dc.language.iso eng
dc.publisher Berlin : Walter de Gruyter
dc.relation.ispartofseries Biological Chemistry 384 (2003), Nr. 7
dc.rights Es gilt deutsches Urheberrecht. Das Dokument darf zum eigenen Gebrauch kostenfrei genutzt, aber nicht im Internet bereitgestellt oder an Außenstehende weitergegeben werden. Dieser Beitrag ist aufgrund einer (DFG-geförderten) Allianz- bzw. Nationallizenz frei zugänglich.
dc.subject beta-carotene eng
dc.subject pleurotus-eryngii eng
dc.subject phanerochaete-chrysosporium eng
dc.subject molecular characterization eng
dc.subject aspergillus-niger eng
dc.subject ionone eng
dc.subject cooxidation eng
dc.subject biotransformation eng
dc.subject lipoxygenase eng
dc.subject proteins eng
dc.subject basidiomycete eng
dc.subject cDNA eng
dc.subject cleavage eng
dc.subject degradation eng
dc.subject norisoprenoids eng
dc.subject.ddc 570 | Biowissenschaften, Biologie ger
dc.subject.ddc 580 | Pflanzen (Botanik) ger
dc.title A peroxidase from Lepista irina cleaves beta,beta-carotene to flavor compounds
dc.type article
dc.type Text
dc.relation.issn 1431-6730
dc.relation.doi http://dx.doi.org/10.1515/BC.2003.117
dc.bibliographicCitation.issue 7
dc.bibliographicCitation.volume 384
dc.bibliographicCitation.firstPage 1049
dc.bibliographicCitation.lastPage 1056
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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