Studies on the inhibition of pancreatic and microbial lipases by soybean proteins.

Y Gargouri,R Julien,G Pieroni,R Verger,L Sarda

doi:10.1016/s0022-2275(20)34465-5

Abstract

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.

Highlights

A protein, molecular weight 70,000 that inhibits pancreatic lipase has been isolated from soybean seeds
Because of the possible relevance of soybean proteins during fat digestion in animals, we have found it of interest to investigate further the inhibitory effect of soybean proteins on lipase activity
We report the isolation from soybean seeds of a protein that inhibits pancreatic lipase activity

Summary

Introduction

A protein, molecular weight 70,000 that inhibits pancreatic lipase has been isolated from soybean seeds. No definite conclusion was attained regarding the biological function of protease and amylase protein inhibitors found in plant materials. Some of these proteins might act as inhibitors of endogenous enzymes and thereby play a repression role in catabolic reactions. Ionic and nonionic detergents can inhibit pancreatic lipase With these synthetic surface-active substances, colipase failed to restore enzymatic activity unless bile salts were added to the assay system [12, 13]. We report the isolation from soybean seeds of a protein that inhibits pancreatic lipase activity

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Conclusion