Purification and Some Properties of a-amylase from Indian Major Carp Catla catla

Abstract

The major amylolytic enzyme of a freshwater fish Catla catla was purified from the hepato- pancreas and characterized as an a-amylase. The a-amylase was purified using ammonium sulphate fractionation and size exclusion chromatography on Sephadex G-100 column. The a-amylase of C. catla was found to have an optimum pH of 6.5. The presence of cal- cium and chloride ions activated the amylase, while EDTA was found to inhibit it. The amylase was determined to be endo-acting by observing the rate of loss of iodine staining power against that of reducing sugar production. The maximum percentage of starch hydrolysis was 60%. The electrophoretic analysis of Sephadex G-100 purified amylase showed only one band on activity staining. The corresponding band obtained in SDS-PAGE was found to have a molecular weight of approximately 86 kD.