Partially hydrolyzed soy protein shows enhanced transport of amino acids compared to nonhydrolyzed protein across an intestinal epithelial cell monolayer.

Consumption of protein hydrolysates has been proposed to stimulate muscle anabolism more than intact (nonhydrolyzed) proteins via accelerated delivery of amino acids for muscle protein synthesis (MPS). We evaluated whether the rate of amino acid uptake and transport across intestinal cells was enhanced for soy protein hydrolysates versus nonhydrolyzed soy protein. Intact and partially hydrolyzed proteins were subject to simulated gut digestion and applied to the apical surface of Caco-2 monolayers. Basolateral media was harvested after 3 h and quantitatively analyzed for free amino acids using ion-exchange chromatography and comparison to an included reference standard. Basolateral concentrations of all amino acids were higher (mean 32%) for hydrolyzed versus nonhydrolyzed protein with the greatest differences in histidine, lysine, and valine. Scale-up production of the soy protein hydrolysate did not diminish its enhanced absorption properties. These data support the hypothesis that hydrolyzed soy protein may provide dietary amino acids that are more rapidly transported across the intestinal epithelium versus intact soy protein. This would be important under conditions where rapid and increased levels of amino acids are needed such as in the stimulation of MPS.

CLIC1 inserts from the aqueous phase into phospholipid membranes, where it functions as an anion channel.

CLIC1 is a member of the CLIC family of proteins, which has been shown to demonstrate chloride channel activity when reconstituted in phospholipid vesicles. CLIC1 exists in cells as an integral membrane protein and as a soluble cytoplasmic protein, implying that CLIC1 might cycle between membrane-inserted and soluble forms. CLIC1 was purified and detergent was removed, yielding an aqueous solution of essentially pure protein. Pure CLIC1 was mixed with vesicles, and chloride permeability was assessed with a chloride efflux assay and with planar lipid bilayer techniques. Soluble CLIC1 confers anion channel activity to preformed membranes that is indistinguishable from the previously reported activity resulting from reconstitution of CLIC1 into membranes by detergent dialysis. The activity is dependent on the amount of CLIC1 added, appears rapidly on mixing of protein and lipid, is inhibited by indanyloxyacetic acid-94, N-ethylmaleimide, and glutathione, is inactivated by heat, and shows sensitivity to pH and to membrane lipid composition. We conclude that CLIC1 in the absence of detergent spontaneously inserts into preformed membranes, where it can function as an anion-selective channel.