Antigenic and some kinetic properties of three p-diphenol oxidase isoenzymes of Trametes versicolor

Production, Purification and Properties of Extracellular Laccase of Agaricus bisporus

“…Multiple electrophoretic forms of other fungal polyphenoloxidases have been shown to be due to small differences in the length and properties of the glycan chains on sub-fractions of the enzyme population (Esser & Minuth, 1971). Similar examples of fungal laccases behaving as single proteins in some separation systems but as multiple forms in others have been reported for Neurospora crassa (Froehner & Eriksson, 1974b), Trametes (Polyporus) versicolor (Jonsson et al, 1968 ;Cheung & Marshall, 1969) and Russulu pseudodelica (Matsubara & Iwasaki, 1972). The broad band of activity found in isoelectric focusing gel columns may also indicate charge heterogeneity of the enzyme population.…”

Purification and characterization of extracellular laccase from Pleurotus ostreatus

“…Many laccases have been reported to be excreted extracellularly as several isozymes (F~hraeus and Reinhammar, 1967;Cheung and Marshall, 1969;Morohoshi et al, 1987;Rehman and Thurston, 1992;Coil et al, 1993). However, the laccase of P. o s t r e a t u s K16-2 appeared as a single activity peak during all chromatography steps.…”

“…Among the ligninolytic enzymes of basidiomycetes, such as laccase, lignin peroxidase, and manganese peroxidase, we have studied laccases, which are found in major white-rot fungi capable of degrading lignin. Extracellular laccases have been purified and characterized from such fungi as Trametes versicolor (Cheung and Marshall, 1969;F~ihraeus and Reinhammar, 1967;Mosbach, 1963;Rogalski et al, 1990), Ganoderma lucidum (Kumari and Sirsi, 1972), Neurospora crassa (Froehner and Eriksson, 1974), Agaricus bisporus (Wood, 1980), Aspergillus nidulans (Kurtz and Champe, 1982), Schizophyllum commune (de Vries et al, 1986), Lentinus edodes (Kofujita et al, 1991 ), Panus tigrinus (Maltseva et al, 1991), Armillaria mellea (Rehman and Thurston, 1992), basidiomycete PM 1 (CECT 2971) (Coil et al, 1993), Cryptococcus neoformans (Williamson, 1994), Trametes villosa (Yaver et al, 1996), and Pycnoporus cinnabarinus (Eggert et al, 1996). Though these laccases have similar molecular weights and similar substrate specificities, they exhibit considerably different amino acid sequences.…”

ESR of Copper in Biological Systems

“…Laccase II, which has a molecular weight of about 70,000, contains 25 % carbohydrate, whereas laccase III has a molecular weight of 80,000 and carbohydrate content of 23 %. The ex-tracellular laccase of Polyporus versicolor can also be resolved into two or possibly three forms (Cheung and Marshall, 1969). The laccase from N. crassa seems to consist of one form of molecular weight 64,800 (Froehner and Eriksson, 1974b).…”