Properties of laccases produced by Pycnoporus sanguineus induced by 2,5-xylidine

Biotechnology Letters
Telma Alves GarciaCirano José Ulhoa

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 degrees C, and Lac II was at pH 4.2 and 50 degrees C over 5 min reaction. The Km values of enzymes toward syringaldazine were 10 microM: (Lac I) and 8 microM: (Lac II). Sodium azide inhibited Lac I (85%) and Lac II (75%) activities.

References

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Citations

Jan 12, 2007·Applied Microbiology and Biotechnology·Telma Alves GarciaCirano José Ulhoa
Nov 1, 2011·Applied Microbiology and Biotechnology·Anne LomascoloLaurence Lesage-Meessen
Oct 20, 2007·Bioresource Technology·M E EugenioJ C Villar
May 5, 2010·Enzyme and Microbial Technology·María I FonsecaLaura L Villalba
Feb 14, 2015·Archives of Microbiology·Ju-Wan ParkHyeon-Su Ro

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