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Physiological phosphatidylcholine protects bovine β‐lactoglobulin from simulated gastrointestinal proteolysis
Author(s) -
Mandalari Giuseppina,
Mackie Alan M.,
Rigby Neil M.,
Wickham Martin S. J.,
Mills E. N. Clare
Publication year - 2009
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.200800321
Subject(s) - proteolysis , chemistry , phosphatidylcholine , biochemistry , proteases , beta lactoglobulin , denaturation (fissile materials) , digestion (alchemy) , in vitro , whey protein , enzyme , chromatography , phospholipid , membrane , nuclear chemistry
We have investigated the effect of phosphatidylcholine (PC) on the resistance of bovine β‐lactoglobulin (β‐Lg) to simulated in vitro gastrointestinal proteolysis. Whilst addition of PC did not affect the resistance of β‐Lg to gastric pepsinolysis, it protected the protein from subsequent degradation under duodenal conditions. The effect was dependent on the ratio of PC to β‐Lg, 16% of the protein remaining intact in the presence of an equimolar ratio of PC/protein, which increased to 62% when a 60‐fold molar excess of PC was included. PC also altered the pattern of digestion products observed by SDS‐PAGE. Thermal denaturation of β‐Lg abolished this effect showing that it was dependent on the native folded structure of the protein. Since neither of the β‐Lg ligands retinol or palmitate exerted a protective effect, it is unlikely that PC is mediating its effect by occupying the central calyx. An alternative explanation may be that the lipids bind to a secondary fatty acid binding site in β‐Lg, thus blocking the action of proteases for steric reasons. These data indicate how biomolecular interactions between proteins and lipids may alter patterns of proteolysis and need to be taken into consideration in any in vitro model of digestion.