Novel peroxidases of Marasmius scorodonius degrade beta-carotene.
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Issue Date
2008-01
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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).Citation
Novel peroxidases of Marasmius scorodonius degrade beta-carotene. 2008, 77 (6):1241-1250 Appl. Microbiol. Biotechnol.Affiliation
Zentrum Angewandte Chemie, Institut für Lebensmittelchemie der Universität Hannover, Wunstorfer Straße 14, 30453, Hannover, Germany.PubMed ID
18038130Type
ArticleISSN
0175-7598ae974a485f413a2113503eed53cd6c53
10.1007/s00253-007-1261-9
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