Purification of α-Amylases Using Magnetic Alginate Beads

1 January 2001

journal article
Published by Springer Nature in Applied Biochemistry and Biotechnology

Vol. 90 (3) , 211-220
https://doi.org/10.1385/abab:90:3:211

Abstract

Magnetic alginate beads were used to purify α-amylases from porcine pancreas, starchzyme, BAN 240L (a commercial purification from Bacillus subtilis), and wheat germ. The beads bound a significant level of α-amylase activity from porcine pancreas, BAN 240L, and wheat germ. In each case, the enzyme activity could be eluted by using 1.0 M maltose, a known competitive inhibitor of α-amylase. In the case of BAN 240L, 3.6-fold purification with 72% recovery of activity was observed. In the case of wheat germ enzyme, starting from the crude extract, 48-fold purification with 70% activity recovery was observed. Sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis also indicated considerable purification in the latter case.

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