Continuous purification of porcine lipase by rotating annular size-exclusion chromatography.
Crude porcine lipase (triacylglycerol lipase, EC 3.1.1.3) was purified in a single-stage chromatographic process. The purification was accomplished in a batch, as well as in a continuous system. Two types of size-exclusion packing materials (Sephadex and Sephacryl) were used. The average x-fold increase in purity, and the average recovered activity in the batch Sephadex and Sephacryl experiments were 13.6 and 89.7%, and 34.2 and 98.8%, respectively. The average x-fold increase in purity and the average activity recovered in the continuous Sephadex and Sephacryl experiments were 27.1 and 82.5% and 16.2 and 89%, respectively. Flow visualization experiments were carried out by tagging the protein to be separated with a fluorescent dye. The results from these experiments are also reported in this article.
Department of Chemical Engineering, University of New Hampshire, Durham 03824, USA.
P W
PW
Genest
T G
TG
Field
P T
PT
Vasudevan
A A
AA
Palekar
D000818:Animals; D002850:Chromatography, Gel / Q000295:instrumentation / Q000379:methods*; D008049:Lipase / Q000302:isolation & purification*; D013552:Swine
D008049:Lipase