Production and partial characterization of elastase of Bacillus subtilis isolated from the cervices of human females.
Conditions are described for the production of extracellular elastase by Bacillus subtilis. The yield of enzyme was maximum in shake-cultures grown in Syncase medium at 37 degrees C and was stable in culture supernatants. The enzyme, purified by ammonium sulphate precipitation and Sephadex G-75 gel filtration, showed a molecular weight of 25,000 and activity between pH 6.0 and 9.5, with an optimum of 9.0 in Tris-maleate buffer. Elastinolytic activity was maximum in glycine-NaOH buffer and minimum in phosphate buffer. Enzyme activity was adversely affected by temperature greater than or equal to 40 degrees C.
D001412:Bacillus subtilis / Q000201:enzymology*; D002584:Cervix Uteri / Q000382:microbiology*; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D003124:Colorimetry; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010196:Pancreatic Elastase / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism
D010196:Pancreatic Elastase