L-Asparaginase activity in Aeromonas sp. isolated from freshwater mussel

Abstract

<i>Aeromonas </i>sp. from <i>Lamellidens marginalis </i>produced <span style="mso-bidi-font-size:11.0pt; font-family:" times="" new="" roman""="">L-asparaginase when grown at 37°C. The optimum enzyme activity was at <i>p</i>H 9 when temperature was 45°C. Half-life of partially purified enzyme at 50°C and 55°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 K_m(<span style="mso-bidi-font-size:11.0pt;font-family:" times="" new="" roman""="">L-asparagine) value of 4.9 ×10^-6 mol 1^-1 and a V_max of 9.803 IU ml^-1. Three metal ions inhibited the enzyme activity at 10-20 μmol^-1 concentrations. Catalytic activity was also inhibited by EDTA, iodoacetic acid, parach

loromercuribenzoic acid and phenylmethylsulphonyl fluoride at 0.1 μ mol 1^-1.

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