Characterization of the bile salt-stimulated lipase in human milk

Abstract

The heat stability of BSSL (bile salt-stimulated lipase) in human milk and colostrum was studied over heating times of 0, 1, 5, 10, 20, 30 and 40 min and heating teperatures of 45, 50, 53, 55 and 60°C. The addition of sodium taurocholate to human milk or colostrum, and the enzyme was completely destroyed at 60°C. No heat inactivation of BSSL was noted at 45°C or below in either milk or colostrum, and the enzyme was completely destroyed at 60°C. The addition of sodium taurocholate to human milk prior to heat treatment had a stabilizing effect on BSSL while the addition fo caffeine to human milk prior to heat treatment had a destabilizing effect on this enzyme. BSSL was partiallypurified using Sephacryl S-300 as the as the separating medium. The molecular weight of BSSL was determined to be 25,000 Daltons. BSSL was confirmed to have the characteristics of a glycoprotein.