S. Bompensieri et al., PURIFICATION OF A LIPASE FROM ACINETOBACTER-CALCOACETICUS AAC323-I BYHYDROPHOBIC-INTERACTION METHODS, Biotechnology and applied biochemistry, 23, 1996, pp. 77-81
The performance of hydrophobic-interaction chromatography (HIC) for th
e purification of Acinetobacter calcoaceticus AAC323-I lipase was comp
ared with that of various aqueous two-phase systems. While a 42% lipas
e yield with a purification factor of 140 could be recovered by HIC, h
igher yields were achieved by using aqueous two-phase systems, either
those formed by poly(ethylene glycol) and dextran or those based upon
the use of a detergent. Triton X-114-based aqueous two-phase partition
showed the best performance, with a yield of 81% and a purification f
actor of 68. Further detergent removal was easily achieved with an ads
orbent, with no significant decrease in yields. Owing to its simplicit
y, the method should be easy to scale-up.