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. 2000 Jul 11;97(15):8717–8722. doi: 10.1073/pnas.140213697

Table 2.

GC measurements of the lipolytic acyl hydrolase activity of maltose-binding protein and lipase fusion protein expressed in E. coli and purified by amylose column chromatography

Substrates Products, μg/mg protein*
Maltose-binding protein Lipase fusion protein
Tri-linolein Linoleic acid (18:2) 15.9 ± 0.75 33.4 ± 1.58
Soybean phospholipid Palmitic acid (16:0) ND§ 4.80
Stearic acid (18:0) ND 9.68
Linoleic acid (18:2) ND 5.80
Dilinoleylphosphatidylcholine Linoleic acid (18:2) ND 20.0
*

Reaction was allowed to proceed for 2 hr and was not continuously linear over this period. 

Means ± SE for n = 3 replications are shown. 

Single experiment. 

§

ND, not detectable.