Related Experiment Video
Updated: Aug 18, 2026

Microfluidic Production of Lysolipid-Containing Temperature-Sensitive Liposomes
Published on: March 3, 2020
Purification of human milk bile salt-activated lipase
Abstract:
A modified procedure for a large-scale purification of human milk bile salt-activated lipase (BAL) has been devised. An initial step used cholate-Sepharose affinity chromatography for the partial purification of the enzyme followed by the removal of cholate with a Bio-Rex 5 anion-exchange resin. The final step of purification used heparin-Sepharose affinity chromatography. This procedure of purification resulted in a 50-fold purification of BAL from human skim milk and a specific activity of 50-60 mumol/min/mg with p-nitrophenyl acetate as substrate. From 450 ml of human skim milk, approximately 30 mg of purified enzyme could be obtained. The N-terminal-region amino acid sequence of the purified BAL was determined as follows: Ala-Lys-Leu-Gly-Ala-Val-Tyr-Thr-Glu-Gly-Lys-Phe-Val-Glu-Gly-Val-Asn-Lys-Lys-Leu-Gly-Leu-. Despite the finding that BAL interacts with heparin-Sepharose, soluble heparin had no effect on BAL activity. The possible physiological role of BAL-heparin interaction has also been discussed.
Related Concept Videos
Lipid Digestion
Detergent Purification of Membrane Proteins
Bile
Bile is released when dietary fats enter...
Lipid Absorption
These breakdown products bind with bile salts and lecithin to form micelles, which quickly pass between microvilli to come in close contact with the apical...

