Studies on the inhibition of pancreatic and microbial lipases by soybean proteins.
A protein, molecular weight 70,000 that inhibits pancreatic lipase has been isolated from soybean seeds. Inhibition is not reversed by colipase unless bile salts are added to the assay system. Inhibitory properties of the purified protein are very similar to those of serum albumin or alpha-lactoglobulin. It has been confirmed that, during intestinal lipolysis of dietary fats, bile salts play an essential role for the activation of the lipase-colipase system in the presence of inhibitory proteins. The purified soybean lipase inhibitory protein was shown to be highly surface-active and able to penetrate monomolecular films of various glycerides and phospholipids at high surface pressure. Inhibition of pancreatic lipase by proteins is related to their capacity to interact with lipids and to modify the quality of the substrate-water interface. The protein isolated from soybeans inhibits pancreatic and Rh. delemar lipase in contrast to the Rh. arrhizus enzyme.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002850:Chromatography, Gel; D006736:Horses; D007700:Kinetics; D008049:Lipase / Q000037:antagonists & inhibitors*; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D010940:Plant Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D012231:Rhizobium / Q000201:enzymology*; D012639:Seeds; D013025:Glycine max; D013045:Species Specificity
D000596:Amino Acids; D010940:Plant Proteins; D008049:Lipase