n-Propanol as a substrate for assaying the ligninperoxidase activity of Phanerochaete chrysoporium.
The steady state kinetics of ligninperoxidase catalysed reaction using n-propanol as the organic substrate and monitoring the formation of propanaldehyde at lambda = 300 nm spectrophotometerically as functions of different reaction parameters has been studied. It has been concluded that n-propanol can be used as a substrate for analysing the activity of ligninperoxidase. The turnover number of ligninperoxidase of Phanerochaete chrysosporium using n-propanol as substrate has been found to be higher approximately by a factor of 10(3) as compared to that using veratryl alcohol as the substrate. The method works in assaying the activity of ligninperoxidase produced by Aspergillus fumigatus indicating that it can be used for assaying the ligninperoxidase activities produced by other microorganisms also and is not limited to assaying the ligninase activity produced by Phanerochaete chrysosporium alone. Under identical experimental conditions, horseradish peroxidase does not show peroxidase activity using n-propanol as substrate indicating that the method does not interfere with the activities of other peroxidases.
Shanmugam
V
V
Department of Chemistry, DDU Gorakhpur University, India.
Kumari
M
M
Yadav
K D
KD
D000433:1-Propanol; D001232:Aspergillus fumigatus / Q000201:enzymology; D001592:Benzyl Alcohols; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010544:Peroxidases / Q000032:analysis* / Q000378:metabolism; D020075:Phanerochaete / Q000201:enzymology*; D013379:Substrate Specificity
D001592:Benzyl Alcohols; D000433:1-Propanol; D010544:Peroxidases; C042858:lignin peroxidase; C042197:veratryl alcohol