Biochemical characterization of the aeromonas species isolated from food and environment

Very few studies have been carried out to comprehensively characterize Aeromonas isolates. This study reports biochemical and enzymatic characterization of 60 isolates belonging to seven Aeromonas species. Seven types of API [Analytab Production Incorporation, France] strips [API 20 E, API 20 NE, Rapid ID 32 E, API 50 CH, ID 32 GN, ID 32 C, Rapid ID 32 A] were used for the biochemical characterization of the isolates. These strips provided an extensive biochemical profile of the isolates. AI 20 E gave reliable results. The H [2] S tubule of this strip was added with gelatin-cysteine-thiosulfate medium and got excellent results for H [2] S production from cysteine. Esculin formulation in ID 32 C was proved most reliable as no false positive or as many false positive and false negative results were given by it. All other strips provided test profile and some of the characteristics in them appeared as significant in differentiation of the various species

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.

Aplicación de la actividad pirazinamidasa para la identificación en especies de Aeromonas / Application of the pyrazinamidase activity for the identification of Aeromonas species

Se ubicaron en especies 70 cepas de Aeromonas aisladas de pacientes con enfermedad diarreica aguda, utilizando las pruebas del factor CAMP y la actividad pirazinamidasa. Se destaca el alto tanto por ciento de coincidencia entre ambas pruebas de fácil realización en los laboratorios de microbiología clínica

Metabolism of proteins and glycoproteins in tumour bearing mice treated with Aeromonas L-asparaginase.

L-asparaginase, isolated in our laboratory, from Aeromonas had been found to be antileukaemic. In the present study, changes in the levels of proteins and glycoproteins in leukaemic mice and under treatment with Aeromonas L-asparaginase have been compared. Levels of protein bound hexose, fucose and sialic acid which were increased during leukaemia attained normal levels when treated with L-asparaginase. The increased blood urea level declined significantly during enzyme therapy. Effects of L-asparaginase are compared with 'Leunase', a commercially available drug used in the treatment of leukaemia.

Production of extracellular proteases and amylases by some acidophilic and alkalophilic bacteria.

Twelve bacteria were isolated from two effluent sources of Shaw-Wallace Gelatins, Jabalpur. Six bacteria from dicalcium phosphate plant effluent (pH-5) and six from main drain of the factory (pH-10) were isolated. Two facultatively acidophilic and two facultatively alkalophilic bacteria were selected and tentatively identified as Plesiomonas shigelloides, Aeromonas hydrophilla, Klebsiella pneumoniae and Staphylococcus saprophyticus respectively. Acidic amylases were produced in higher amounts on 4th day of incubation by Plesiomonas shigelloides and on 6th day by Aeromonas hydrophilla. Alkaline amylases were produced in higher amounts on 4th day of incubation by Klebsiella pneumoniae and on 8th day by Staphylococcus saprophyticus in vitro.