L-asparaginase activity in Aeromonas sp. isolated from freshwater mussel.
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.
Pattnaik
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S
Pearl Culture Section, Central Institute of Freshwater Aquaculture, ICAR, Kausalyaganga, Bhubaneswar, 751 002, India.
Kabi
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Janaki Ram
K
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Bhanot
K K
KK
D000333:Aeromonas / Q000201:enzymology*; D000818:Animals; D001215:Asparaginase / Q000378:metabolism*; D049872:Bivalvia / Q000382:microbiology*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000378:metabolism
D008670:Metals; D001215:Asparaginase