Magnetite-alginate beads for purification of some starch degrading enzymes
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Starch degrading enzymes, viz., β-amylase, glucoamylase, and pullulanase, were purified using magnetite-alginate beads. In each case, the enzyme activity was eluted by using 1.0 M maltose. β-Amylase (sweet potato), glucoamylase (Aspergillus niger), and pullulanase (Bacillus acidopullulyticus) from their crude preparations were purified 37-, 31-, and 49-fold with 86, 87, and 95% activity recovery, respectively.
Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed single band in each case.
Index EntriesAffinity separation β-amylase glucoamylase pullulanase magnetite-alginate beads Aspergillus niger Bacillus acidopullulyticus
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- 5.Safarik, I. and Safarikova, M. (1997) Overview of magnetic separations used in biochemical and biotechnological applications, in Scientific and Clinical Applications of Magnetic Carriers (Hafeli, U., Schut, W., Teller, J., and Dorowski, M., eds.), Plenum Press, New York, pp. 323–340.Google Scholar
- 6.Tyagi, R. and Gupta, M.N. (1995) Purification and immobilization of Aspergillus niger on magnetic latex beads. Biocatal. Biotrans. 12, 293–298.Google Scholar
- 12.Bernfeld, P. (1955) Amylases α and β, in Methods in Enzymology, Vol. 1 (Colowick, S. P. and Kaplan, N., eds), Academic Press, New York, pp. 149–158.Google Scholar
- 13.Nelson, N. (1944) Photometric adaptation of the Somogyi method for the determination of glucose. J. Biol. Chem. 153, 375–380.Google Scholar
- 15.Hames, B. D. (1986) An Introduction to polyacrylamide gel electrophoresis, in Gel Electrophoresis of Protein; A Practical Approach, (Hames, B. D. and Rickwood, D. eds), IRL Press, Oxford, pp. 1–86.Google Scholar
- 17.Manjunath, P. and Raghavendra Roa, M. R. (1979) Comparative studies on glucoamylases from three sources. J. Biosci. 1, 409–425.Google Scholar
- 21.Patil, V. B., Patil, N. B. (2000) Biomass conversion: Synergistic use of α-amylase and amyloglucosidase for rapid and maximum conversion of starch into glucose. Ind. J. Chem. Technol. 7, 47–50.Google Scholar