Abstract
Thiaminase I from Clostridium sporogenes ATCC 8075 was purified 9,100 fold over its culture fluids by the following methods : Norit A treatment, calcium phosphate gel adsorption, ammonium sulfate precipitation, gel filtration and cation and anion exchange column chromatography. The purity of the enzyme preparation in each purification step was checked by means of disc elctrophoresis. The purified enzyme had a specific activity of 61.0 units per mg of protein at pH 8.0,30℃, and the molecular weight determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate was 42,000.
