Isolation and Characterization of Purified Bile Salt Stimulated Human Milk Lipase

Abstract

A method has been developed for the isolation and purification of bile-salt-stimulated human milk lipase. This method yields up to six times more enzyme than other reported methods and the specific activity is compara ble. The concentration of BSSL recovered from the whole milk was 0.65 percent of the original protein content. The molecular weight of the isolated protein was 120 kDa. During the course of the purification, both protein content and specific activity were monitored and the esterase and lipase activities of the isolated product were characterized in the presence of sodium taurocholate. Five separate isolations were carried out with the introduction of minor varia tions in the procedure, but the catalytic properties of the product remain unchanged.