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.
Tripathi
K K
KK
Department of Microbiology, Panjab University, Chandigarh-, India.
Kaur
M
M
Gupta
M
M
Gupta
K G
KG
D002850:Chromatography, Gel; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010196:Pancreatic Elastase / Q000032:analysis / Q000096:biosynthesis* / Q000302:isolation & purification; D013696:Temperature; D014734:Vibrio cholerae / Q000201:enzymology*
D003470:Culture Media; D010196:Pancreatic Elastase