Production and partial characterization of elastase of Vibrio cholerae Inaba

Conditions are described for the production of extracellular elastase by Vibrio cholerae Inaba 2/57. The yield of the enzyme was maximum in shake cultures grown in alkaline peptone water at 37 degrees C and was stable in culture supernatants. The enzyme, partially purified by ammonium sulphate precipitation and Sephadex G-100 gel filtration showed a molecular weight of 30,000 and an activity between pH 5.0-8.0 with an optimum of 8.0 in Tris-maleate buffer. The elastinolytic activity was maximal in glycine-NaOH buffer and minimal in phosphate buffer. The enzyme activity was adversely affected by temperature greater than or equal to 40 degrees C.