PuriWcation of bacterial lipase by ion-exchange
chromatography
A column (size 12£2cm, VtD36.7 cm3) was packed with
DEAE–Cellulose (Sigma Chemical, USA). The matrix was
activated sequentially with 0.1N HCl and 0.1N NaOH.
Subsequently, column was equilibrated with 0.02M phosphate
buVer (pH 7.4). The crude enzyme (2 ml of enzyme
concentrated by lyophilization t40.2mg protein) after dialysis
against 0.005 M phosphate buVer (pH 7.5) was loaded on the column.