Abstract
The pink and yellow pigments of Pleurotus salmoneostramineus L. Vass. were separated by gel filtration. The pink pigment was purified as a chromoprotein by purification procedures that included successive ammonium sulfate fractionation and DEAE-Toyopearl and Toyopearl HW55 column chromatography. A single protein band was observed following SDS-PAGE, and its molecular mass was estimated to be approximately 24.5 kDa. The relative molecular mass of the native chromoprotein, as estimated based on its behavior in high-performance liquid chromatography-gel permeation chromatography (HPLC-GPC), was approximately 30 kDa. The chromoprotein was stable against heating at 28℃ for 30 min and at pH values between 4 and 10. The major absorption maxima of the chromoprotein were observed at 267, 348, and 493 nm. The three yellow pigments were purified by repeated gel filtration on Sephadex G-25 columns. The molecular masses of the yellow pigments were estimated by HPLC-GPC as 10.8, 5.3 and 4.4 kDa. None of the isolated yellow pigments showed specific maximum absorption in the visible region, and all of the yellow pigments were soluble only in water. The pigments were bleached by H_2O_2, KMnO_4, and NaOCl, and reduced Fe^<3+> to Fe^<2+>. These characteristics are consistent with those of melanin pigments.
