Table 1.

Spectrophotometric 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

Protein species	Product
	p-nitrophenol	Free fatty acid
Maltose-binding protein	0.71  ± 0.02	ND
Lipase fusion protein	12.02  ± 1.81	46.75  ± 1.24

Two substrates, p-nitrophenylpalmitate and soybean phospholipid, were used. Activities are expressed as nanomoles of product formed (p-nitrophenol from p-nitrophenylpalmitate and free fatty acid from soybean phospholipid)/milligrams of protein/minute. Means ± SE for n = 3 replications are shown. ND, not detectable.