A Highly Efficient Recombinant Laccase from the Yeast Yarrowia lipolytica and Its Application in the Hydrolysis of Biomass
Fig 1
Determination of the molecular mass of purified YlLac by (a) SDS-PAGE of laccase (M, Marker; L1, Crude protein; L2, endoglycosidase-H-treated YlLac); and (b) zymogram activity and glycoprotein staining of the purified laccase enzyme with native PAGE (L1, ABTS; L2, 2,6-DMP; L3, glycoprotein staining).
The zymogram process was carried out using native PAGE, and the enzyme band was visualized by incubating the gel in 50 mM sodium acetate buffer (pH 4.8) containing 0.1 mM ABTS and 2,6-DMP at room temperature.