Open AccessPurification and characterization of lignin peroxidase from Loweporus lividus MTCC‐1178
Author(s) -
Yadav Meera,
Yadav Pratibha,
Yadav Kapil Deo Singh
Publication year - 2009
Publication title -
engineering in life sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.547
H-Index - 57
eISSN - 1618-2863
pISSN - 1618-0240
DOI - 10.1002/elsc.200800084
Subject(s) - lignin , peroxidase , lignin peroxidase , chemistry , cellulose , enzyme , substrate (aquarium) , chromatography , alcohol , organic chemistry , biochemistry , biology , ecology
Lignin peroxidase from the culture filtrate of Loweporus lividus MTCC‐1178 has been purified to homogeneity using Amicon concentration and DEAE cellulose chromatography. The molecular weight of the purified lignin peroxidase using SDS‐PAGE analysis has been found to be 40 kDa. The K m values for veratryl alcohol and H 2 O 2 for the purified enzyme were 58 and 83 μM, respectively. The calculated k cat value of the purified enzyme using veratryl alcohol as the substrate was 2.5 s −1 . The pH and temperature optima of lignin peroxidase have been found to be 2.6 and 24°C, respectively.