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Macroaffinity Ligand‐Facilitated Three‐Phase Partitioning (MLFTPP) of α‐Amylases Using a Modified Alginate
Author(s) -
Mondal Kalyani,
Sharma Aparna,
Gupta Munishwar Nath
Publication year - 2003
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp025619e
Subject(s) - amylase , bacillus amyloliquefaciens , ammonium sulfate , maltose , chemistry , ammonium , ligand (biochemistry) , phase (matter) , chromatography , sucrose , biochemistry , enzyme , organic chemistry , receptor , fermentation
The crude extracts of α‐amylases when mixed with alginate, tert ‐butyl alcohol, and ammonium sulfate resulted in an interfacial precipitate containing polymer‐bound amylase. The precipitate was dissolved in 1 M maltose to recover α‐amylase activity. The recovery of α‐amylases were 74%, 77%, and 92% in the case of Bacillus amyloliquefaciens, wheat germ, and porcine pancreas, respectively. All purified preparations showed a single band on SDS‐PAGE.