Purification, kinetics and spectral characterisation of a new versatile peroxidase from a Bjerkandera sp isolate

• Type: Article in International Scientific Journal
• Date: 2006

Authors

Moreira, PR (Author) Other; Bouillenne, F (Author) Other; Almeida Vara, E (Author) Other; F. Xavier Malcata (Author) Other; Frere, JM (Author) Other; Duarte, JC (Author) Other

Journal

Title: Enzyme and Microbial Technology

Vol. 38

Pages: 28-33

ISSN: 0141-0229

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 31 Citations

Scopus - 37 Citations

Other information

Authenticus ID: P-004-NQR

DOI: 10.1016/j.enzmictec.2004.12.035

Abstract (EN): From the extracellular fluid of a novel strain of Bjerkandera sp., it was isolated, purified and identified the main enzyme responsible for Remazol Brilliant Blue R dye decolourisation. Such an enzyme is able to oxidise manganese, as well as veratryl alcohol and 2,6-dimethoxyphenol in manganese-independent reactions; hence, it can be included in the new group of versatile peroxidases. The molecular mass of said enzyme is ca. 45 kDa, and the N-terminal amino acid sequence obtained by Edman degradation is VAXPDGVNTA. The enzyme substrate range for oxidation of several phenolic and non-phenolic aromatic compounds was determined and the corresponding Michaelis-Menten kinetic constants calculated. Furthermore, spectrophotometric assays showing the Soret band and allowing observation of band shifts of the enzyme led to the conclusion that Bjerkandera strains may also synthesise at least two different versatile peroxidases, as happens with Pleurotus eryngii.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6