ABSTRACT
Triacylglycerol ester hydrolase was isolated from bat adipose tissue and characterized. The partially purified enzyme had pH optimum of 8.6 and a Km value of 0.6 mM. The enzyme was denaturated upon freezing and thawing, which was prevented by 25% glycerol. The enzyme was activated by EDTA and NaCl, while it was inhibited by serum and bovine serum albumin. Heparin, sodium fluoride and diisopropyl fluorophosphate had no effect on triacylglycerol ester hydrolase activity. It hydrolyzed triglycerides partially. Triacylglycerol ester hydrolase lost its activity during delipidation but it was reactivated by endogenous lipids and phospholipids, viz. phosphatidyl ethanolamine, phosphatidyl choline and sphingomyelin. The enzyme shows kinetic properties altogether different from lipoprotein lipase and hormone sensitive lipase.