L-asparaginase activity in Aeromonas sp. isolated from freshwater mussel.
No Thumbnail Available
Date
2000-11-09
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
Aeromonas sp. from Lamellidens marginalis produced L-asparaginase when grown at 37 degrees C. The optimum enzyme activity was at pH 9 when temperature was 45 degrees C. Half-life of partially purified enzyme at 50 degrees C and 55 degrees C was 35 and 20 min, respectively. Activation and deactivation energies of partially purified enzyme were 17.48 and 24.86 kcal mol-1 respectively. The enzyme exhibited a Km (L-asparagine) value of 4.9 x 10(-6) mol l-1 and a Vmax of 9.803 IU ml-1. Three metal ions inhibited the enzyme activity at 10-20 mumol l-1 concentrations. Catalytic activity was also inhibited by EDTA, iodoacetic acid, parachloromercuribenzoic acid and phenylmethylsulphonyl fluoride at 0.1 mumol l-1.
Description
Keywords
Citation
Pattnaik S, Kabi R, Janaki Ram K, Bhanot KK. L-asparaginase activity in Aeromonas sp. isolated from freshwater mussel. Indian Journal of Experimental Biology. 2000 Nov; 38(11): 1143-6