Applied Biochemistry and Biotechnology

, Volume 90, Issue 3, pp 211–220

Purification of α-amylases using magnetic alginate beads


DOI: 10.1385/ABAB:90:3:211

Cite this article as:
Teotia, S. & Gupta, M.N. Appl Biochem Biotechnol (2001) 90: 211. doi:10.1385/ABAB:90:3:211


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.

Index Entries

Affinity separationα-amylasemagnetic alginate beadsmacroaffinity ligandswheat amylase

Copyright information

© Humana Press Inc. 2001

Authors and Affiliations

  1. 1.Chemistry DepartmentIndian Institute of Technology, Delhi, Hauz KhasNew DelhiIndia