2.50
HDL Handle:
http://hdl.handle.net/10033/22933
Title:
Novel peroxidases of Marasmius scorodonius degrade beta-carotene.
Authors:
Scheibner, M; Hülsdau, B; Zelena, K; Nimtz, M; de Boer, L; Berger, RG; Zorn, H
Abstract:
Two extracellular enzymes (MsP1 and MsP2) capable of efficient beta-carotene degradation were purified from culture supernatants of the basidiomycete Marasmius scorodonius (garlic mushroom). Under native conditions, the enzymes exhibited molecular masses of ~150 and ~120 kDa, respectively. SDS-PAGE and mass spectrometric data suggested a composition of two identical subunits for both enzymes. Biochemical characterisation of the purified proteins showed isoelectric points of 3.7 and 3.5, and the presence of heme groups in the active enzymes. Partial amino acid sequences were derived from N-terminal Edman degradation and from mass spectrometric ab initio sequencing of internal peptides. cDNAs of 1,604 to 1,923 bp, containing open reading frames (ORF) of 508 to 513 amino acids, respectively, were cloned from a cDNA library of M. scorodonius. These data suggest glycosylation degrees of ~23% for MsP1 and 8% for MsP2. Databank homology searches revealed sequence homologies of MsP1 and MsP2 to unusual peroxidases of the fungi Thanatephorus cucumeris (DyP) and Termitomyces albuminosus (TAP).
Affiliation:
Zentrum Angewandte Chemie, Institut für Lebensmittelchemie der Universität Hannover, Wunstorfer Straße 14, 30453, Hannover, Germany.
Citation:
Novel peroxidases of Marasmius scorodonius degrade beta-carotene. 2008, 77 (6):1241-1250 Appl. Microbiol. Biotechnol.
Journal:
Applied microbiology and biotechnology
Issue Date:
Jan-2008
URI:
http://hdl.handle.net/10033/22933
DOI:
10.1007/s00253-007-1261-9
PubMed ID:
18038130
Type:
Article
Language:
ISSN:
0175-7598
Appears in Collections:
Publications from RG Biophysical Analysis (BA)

Full metadata record

DC FieldValueLanguage
dc.contributor.authorScheibner, M-
dc.contributor.authorHülsdau, B-
dc.contributor.authorZelena, K-
dc.contributor.authorNimtz, M-
dc.contributor.authorde Boer, L-
dc.contributor.authorBerger, RG-
dc.contributor.authorZorn, H-
dc.date.accessioned2008-04-10T14:42:13Z-
dc.date.available2008-04-10T14:42:13Z-
dc.date.issued2008-01-
dc.identifier.citationNovel peroxidases of Marasmius scorodonius degrade beta-carotene. 2008, 77 (6):1241-1250 Appl. Microbiol. Biotechnol.en
dc.identifier.issn0175-7598-
dc.identifier.pmid18038130-
dc.identifier.doi10.1007/s00253-007-1261-9-
dc.identifier.urihttp://hdl.handle.net/10033/22933-
dc.description.abstractTwo extracellular enzymes (MsP1 and MsP2) capable of efficient beta-carotene degradation were purified from culture supernatants of the basidiomycete Marasmius scorodonius (garlic mushroom). Under native conditions, the enzymes exhibited molecular masses of ~150 and ~120 kDa, respectively. SDS-PAGE and mass spectrometric data suggested a composition of two identical subunits for both enzymes. Biochemical characterisation of the purified proteins showed isoelectric points of 3.7 and 3.5, and the presence of heme groups in the active enzymes. Partial amino acid sequences were derived from N-terminal Edman degradation and from mass spectrometric ab initio sequencing of internal peptides. cDNAs of 1,604 to 1,923 bp, containing open reading frames (ORF) of 508 to 513 amino acids, respectively, were cloned from a cDNA library of M. scorodonius. These data suggest glycosylation degrees of ~23% for MsP1 and 8% for MsP2. Databank homology searches revealed sequence homologies of MsP1 and MsP2 to unusual peroxidases of the fungi Thanatephorus cucumeris (DyP) and Termitomyces albuminosus (TAP).en
dc.languageENG-
dc.language.isonullen
dc.titleNovel peroxidases of Marasmius scorodonius degrade beta-carotene.-
dc.typeArticleen
dc.contributor.departmentZentrum Angewandte Chemie, Institut für Lebensmittelchemie der Universität Hannover, Wunstorfer Straße 14, 30453, Hannover, Germany.en
dc.identifier.journalApplied microbiology and biotechnologyen

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