ISOLATION AND CHARACTERIZATION OF PURIFIED BILE-SALT STIMULATED HUMAN-MILK LIPASE

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 comparable. The concentration of BSSL recovered from the whole milk wa s 0.65 percent of the original protein content. The molecular weight o f the isolated protein was 120 kDa. During the course of the purificat ion, both protein content and specific activity were monitored and the esterase and lipase activities of the isolated product were character ized in the presence of sodium taurocholate. Five separate isolations were carried out with the introduction of minor variations in the proc edure, but the catalytic properties of the product remain unchanged.