[Optimization of conditions for immobilization of alpha-amylase from Bacillus sp. BKL20 in Ca2+-alginate beads].
The method of alpha-amylase from Bacillus sp. immobilization by an entrapment in Ca2+-alginate beads has been performed in the paper. Maximum content of immobilized alpha-amylase was observed at neutral pH values during immobilization. The approximately equal quantities of alpha-amylase were entrapped into Ca2+-alginate beads, that was confirmed by the similar total activity (approximately 0.05 U) and declining specific activity (from 12 to 1 U/mg protein) of immobilized alpha-amylase after the addition of different amounts of enzyme preparation (from 20 to 160 mg of protein) to 1 ml of 2% alginate solution. Alginate concentration affected the activity of immobilized enzyme, maximum alpha-amylase activity was observed at low concentrations of the carrier (0.15-0.25%), used to prepare beads. alpha-Amylase, entrapped in Ca2+-alginate beads, was successfully tested during five hydrolysis cycles.
O I
OI
Kubrak
V I
VI
Lushchak
D000464:Alginates / Q000737:chemistry*; D001407:Bacillus / Q000201:enzymology*; D001709:Biotechnology / Q000379:methods*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D020723:Glucuronic Acid / Q000737:chemistry; D006603:Hexuronic Acids / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008863:Microspheres; D000516:alpha-Amylases / Q000302:isolation & purification / Q000378:metabolism*
D000464:Alginates; D004800:Enzymes, Immobilized; D006603:Hexuronic Acids; D020723:Glucuronic Acid; D000516:alpha-Amylases