IMMOBILIZATION OF ALPHA-AMYLASE FROM MYCELIOPHTHORA-THERMOPHILA D-14 (ATCC-48104)

Different techniques for immobilization of partially purified alpha-am ylase from Myceliophthora thermophila D-14 were studied to maximize th e rate of conversion of starch to glucose. The enzyme was covalently b ound to CNBr-activated Sepharose and entrapped within crosslinked poly acrylamide gels and calcium-alginate beads. Of the three gels, Ca-algi nate beads proved to be the best carrier for immobilization. The immob ilized enzyme showed marked improvement in operational as well as stor age stability. The enzyme activity attained its maximum at 60-degrees- C for soluble and 65-degrees-C for immobilized enzymes. In addition, t he operational pH range of the immobilized preparation was increased. Results of repeated batch experiments suggested that the immobilized e nzymes could be reused.