Publications (2)1.27 Total impact
Article: Interference of laccase in determination of cellobiose dehydrogenase activity of Pleurotus ostreatus (Florida) using dichlorophenol indophenol as the electron acceptor.[show abstract] [hide abstract]
ABSTRACT: Pleurotus ostreatus (Florida), ITCC 3308 produces approximately 9.0 U/ml extracellular cellobiose dehydrogenase (CDH) in cellulose medium after 7 days of growth. However, no activity could be detected if the assay was done with cellobiose as the substrate and 2,6-dichlorophenol indophenol (DPIP) as the electron acceptor in absence of any laccase inhibitor. Kinetic study showed that V(max)/K(m) value was very high for rDPIP (reduced 2,6-dichlrophenol indophenol) oxidation by laccase. Oxygen consumption rate of rDPIP oxidation by the enzyme was found to be highest among all the tested substrates. The present study indicated that rDPIP was a good substrate for laccase. Therefore, caution is needed to measure CDH activity by monitoring DPIP reduction in a system where laccase is likely to be present.Journal of Basic Microbiology 02/2005; 45(2):142-6. · 1.27 Impact Factor
Article: Cellobiose dehydrogenase production by the mycelial culture of the mushroom Termitomyces clypeatus[show abstract] [hide abstract]
ABSTRACT: Termitomyces clypeatus produces cellobiose dehydrogenase (CDHtc) in cellulose medium with the highest yield (55.88 U mL−1) among all the reported fungal species. The enzyme has been isolated and purified from the culture filtrate.CDHtc was found to be a very thermolabile enzyme with the temperature optimum at 30 °C, while it exhibited a wide range of pH stability from pH 2.0 to 8.0. Lactose was efficiently converted to lactobionic acid in presence of the enzyme. Addition of glucose in the cellulose medium on the first day of growth induced a lag period in enzyme production but ultimately facilitated earlier CDHtc production and the yield was also comparable to that achieved in the cellulose medium.Process Biochemistry.