APPLICATION OF PROTEOLYTIC ENZYMES IN SUPPRESSING IMMUNOREACTIVITY AND DEACTIVATION OF ANTIGENIC EPITOPES IN THE WHEY PROTEIN ISOLATE
Date
2017-04-13T11:53:38Z
Authors
Torabi zadeh, Maryam
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Abstract
Whey protein is a by-product of cheese manufacturing and a rich source of bioactive peptides. However, it is an important cause of food allergy in many patients that are allergic to bovine milk. Enzymatic hydrolysis is an approach that has been used for the production of hypoallergenic products. The impact of hydrolysis with various enzymes on immunochemical properties, hydrophobicity and particle size of whey protein isolate was studied. Twelve different enzymes were used of which papain and pancreatin hydrolysate showed the highest immunoglobulin (Ig) E inhibition of 47% and 45% among all the hydrolysates. A strong negative correlation between the degree of hydrolysis and hydrophobicity was observed. The peptidomics result of papain hydrolysate was analyzed and enzymatic cleavage sites were determined. Comparison of in silico and actual results indicated that antigenic epitopes were mostly degraded. This demonstrates antigenic inhibition in the papain whey hydrolysate obtained in vitro.
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Whey protein, Enzymatic hydrolysis, Cleavage specificity, Antigenic epitopes, Suppressing immunoreactivity, Peptidomics, Papain hydrolysate, Whey, Whey products