Properties of Laccases Produced by Pycnoporus sanguineus Induced by 2,5-xylidine |
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| Authors: | Telma Alves Garcia Mariângela Fontes Santiago Cirano José Ulhoa |
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| Affiliation: | (1) Instituto Ciências Biológicas, Faculdade de Farmácia, Universidade Federal de Goiás, 74001-970 Goiania, GO, Brazil;(2) Instituto de Biologia, Universidade de Brasília, Campus Asa Norte, 70.910-900 Brasília, DF, Brazil |
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| Abstract: | Two isoforms of laccase produced from the culture supernatant of Pycnoporus sanguineus were partially purified by phenyl-Sepharose chromatography. Molecular masses of the enzymes were 80 kDa (Lac I) and 68 kDa (Lac II). Optimum activity of Lac I was at pH 4.8 and 30 °C, and Lac II was at pH 4.2 and 50 °C over 5 min reaction. The Km values of enzymes toward syringaldazine were 10 μm (Lac I) and 8 μm (Lac II). Sodium azide inhibited Lac I (85%) and Lac II (75%) activities. Revisions requested 30 November 2005; Revisions received 26 January 2006 |
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| Keywords: | isoforms characterization laccase Pycnoporus sanguineus |
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