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Purification and characterization of a growth‐regulating laccase from Pleurotus florida
Author(s) -
Das Nirmalendu,
Chakraborty Tapas K.,
Mukherjee Mina
Publication year - 2001
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/1521-4028(200110)41:5<261::aid-jobm261>3.0.co;2-v
Subject(s) - laccase , copper , size exclusion chromatography , molecular mass , enzyme , pleurotus , chemistry , chromatography , fungus , pleurotus ostreatus , biochemistry , food science , biology , botany , organic chemistry , mushroom
Pleurotus florida produces two laccase enzymes (L 1 and L 2 ) within which L2 is associated with the vegetative growth of the fungus. In the present investigation the L 2 has been purified to homogeneity and characterized. The molecular mass of the enzyme has been determined to be 73 kDa and 70 kDa by gel filtration chromatography and SDS‐PAGE, respectively. The purified enzyme shows a pI value of 4.2. The optimum reaction temperature is 50 °C. Spectroscopic analysis reveals that L 2 has two copper atoms, a type I copper and a type II copper. The K m and some other kinetic parameters of L 2 has been determined.