RESUMEN
A polyamide with the covalently coupled phosphatidyl ethanolamine was used for affinity adsorption of an alkaline lipase from Pseudomonas aeruginosa. The immobilization resulted in increase of the enzyme specific activity. Some properties of native and adsorbed enzyme were compared. The temperature optima, heat and pH stability, KM and Vmax values were determined for both native and immobilized enzymes.
Asunto(s)
Enzimas Inmovilizadas , Lipasa/metabolismo , Pseudomonas aeruginosa/enzimología , Concentración de Iones de Hidrógeno , Hidrólisis , Cinética , Fosfatidiletanolaminas/metabolismo , Especificidad por Sustrato , TemperaturaRESUMEN
The paper gives data on the influence of different sources of carbon, nitrogen and phosphorus on the accumulation of biomass and synthesis of neutral protease by Bacillus subtilis str. 103. The highest proteolytic activity was obtained on the medium containing maltose or hydrolyzed starch as a carbon source, monopotassium phosphate as a phosphorus source, and ammonium sulphate as a nitrogen source. The enzyme activity increased upon an addition of albumin, peptone or casein. A study of the amino acid effect showed that methionine, isoleucine and valine stimulated the protease synthesis to the greatest extent.