Abstract
ABSTRACTControlled partitioning of a commercial α-amylase is achieved in aqueous biphasic system (ABS) of a hydrophobic and polar ionic liquid, 3-methyl-1-octylimidazol-3-ium saccharinate ([C8C1im][Sac]). Studying the effects of pH and [C8C1im][Sac]-concentration, the IL interference in the amylolytic action is deduced. Liquid–liquid extractions into [C8C1im][Sac] at different pHs are carried out. The α-amylase extraction occurs below pH = pI (isoelectric point), and above pI other inactive proteins are preferably transferred. The extracted α-amylase is afterwards recovered, being partially purified from inactive protein and microbial pigment. In the ABSs of pHs > pI, the α-amylase remains concentrated and purified in the aqueous raffinates.
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