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 K m 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.
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Revisions requested 30 November 2005; Revisions received 26 January 2006
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Garcia, T.A., Santiago, M.F. & Ulhoa, C.J. Properties of Laccases Produced by Pycnoporus sanguineus Induced by 2,5-xylidine. Biotechnol Lett 28, 633–636 (2006). https://doi.org/10.1007/s10529-006-0026-3
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DOI: https://doi.org/10.1007/s10529-006-0026-3