抄録
Succeeding to our previous reports, purification of thiaminase II was attempted by ion exchange resins and ammonium sulfate partition. Cation exchanger (Amberlite IR-120) and Anion exchanger (Amberlite IRA-400) were used in mixed (1 : 2) or separated column. Purified thiaminase II was obtained from precipitation at 40〜45% saturation of ammonium sulfate in resin treated enzyme solution. Purified enzyme required chelating reagents such as EDTA for enzymatic action, and was comparatively stable for the temperature (less than 55℃).
