Abstract
Amylase (E.C.3.2.1.1) and acid phosphatase (E.C.3.1.3.2) from sugar cane juice have been isolated and purified by salt and solvent fractionation. They have been separated by ion-exchange chromatography using DEAE cellulose and phosphocellulose columns and were immobilized on tricalcium phosphate gel. Some of the properties of immobilized and free soluble enzymes have been compared. The pH and temperature profiles of free and immobilized amylase and acid phosphatase did not show much alteration. Thermal stability of both the enzymes increased in the presence of 18% sucrose solution. The K m value of amylase and acid phosphatase increased on immobilization, while the V max values showed wide variation. Application of co-immobilized amylase and acid phosphatase in the removal of starch from cane juice has been suggested.
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