Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/2392

TitleAn acid-stable laccase from sclerotium rolfsii with potential for wool dye decolourization
Author(s)Ryan, S.
Schnitzhofer, W.
Tzanov, Tzanko
Paulo, Artur Cavaco
KeywordsLaccase
Purification
Characterization
Sclerotium rolfsii
Issue dateNov-2003
PublisherElsevier
JournalEnzyme and Microbial Technology
Citation"Enzyme and microbial technology". ISSN 0141-0229. 33:6 (Nov. 2003) 766–774.
Abstract(s)The plant pathogen basidiomycete S. rolfsii secretes two laccases (SRL1 and SRL2) with molecular weights of 55 and 86 kDa, respectively. Laccase production was shown to be inducible by the addition of 2,5-xylidine to the cultural media. After treatment with a combination of chitinase and -1,3-glucanase, two different laccases were isolated from the sclerotia depending on the stage of sclerotia development. The more prominent laccase, SRL1, was purified and found to decolourize the industrially important wool azo dye Diamond Black PV 200 without the addition of redox mediators. The enzyme (pI 5.2) was active in the acidic pH range, showing an optimal activity at pH 2.4, with ABTS as substrate. The optimum temperature for activity was determined to be 62 ◦C. Enzyme stability studies revealed that SRL1 was notably stable at 18 ◦C and pH 4.5, retaining almost full activity after a week. Oxidation of tyrosine was not detectable under the reaction conditions but the enzyme did oxidize a variety of the usual laccase substrates. SRL1 was strongly inhibited by sodium azide and fluoride. Dye solutions decolourized with the immobilized laccase were successfully used for redyeing.
TypeArticle
URIhttp://hdl.handle.net/1822/2392
DOI10.1016/S0141-0229(03)00162-5
ISSN0141-0229
Peer-Reviewedyes
AccessOpen access
Appears in Collections:DET/2C2T - Artigos em revistas internacionais com arbitragem científica

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