Properties of laccases produced by Pycnoporus sanguineus induced by 2,5-xylidine.
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.
Garcia
Telma Alves
TA
Instituto Ciências Biológicas, Faculdade de Farmácia, Universidade Federal de Goiás, Goiânia, GO, Brazil.
Santiago
Mariângela Fontes
MF
Ulhoa
Cirano José
CJ
D001709:Biotechnology; D002847:Chromatography, Agarose; D004790:Enzyme Induction / Q000187:drug effects; D004795:Enzyme Stability; D006835:Hydrazones / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D042845:Laccase / Q000096:biosynthesis* / Q000737:chemistry / Q000378:metabolism; D008970:Molecular Weight; D011124:Polyporaceae / Q000187:drug effects* / Q000201:enzymology*; D013379:Substrate Specificity
D006835:Hydrazones; D007527:Isoenzymes; C009370:syringaldazine; D042845:Laccase