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Proteins inhibiting pancreatic lipase in vitro have been isolated from wheat germ and wheat bran, with relative molecular mass ranging from 24,400 to 27,500. Inhibition of pancreatic lipase by the wheat germ proteins is related to their ability to interact with the emulsified substrate and to hinder the adsorption of the enzyme on the interface. The extent of inhibition depends on the amount of substrate and is independent of the enzyme concentration. Bile salts forming micelles in the concentration range used are able to partially reverse the inhibition of pancreatic lipase by the wheat germ proteins. The nutritional significance of the data obtained is discussed.
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