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Purification of a lipase from Acinetobacter calcoaceticus AAC323‐1 by hydrophobic‐interaction methods
Author(s) -
Bompensieri S.,
Gonzalez R.,
Kok R.,
MV Miranda,
NutgerenRoodzant I.,
KJ Hellingwerf,
Cascone O.,
BC Nudel
Publication year - 1996
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1996.tb00366.x
Subject(s) - acinetobacter calcoaceticus , lipase , chromatography , chemistry , yield (engineering) , partition coefficient , ethylene glycol , adsorption , aqueous solution , triacylglycerol lipase , aqueous two phase system , hydrophilic interaction chromatography , peg ratio , acinetobacter , high performance liquid chromatography , organic chemistry , enzyme , materials science , biochemistry , finance , economics , metallurgy , antibiotics
The performance of hydrophobic‐interaction chromatography (HIC) for the purification of Acinetobacter calcoaceticus AAC323‐1 lipase was compared with that of various aqueous two‐phase systems. While a 42% lipase yield with a purification factor of 140 could be recovered by HIC, higher 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 factor of 68. Further detergent removal was easily achieved with an adsorbent, with no significant decrease in yields. Owing to its simplicity, the method should be easy to scale‐up.