Comparative study of in vitro digestibility of food proteins and effect of preheating on the digestion.

Abstract

Information on the comparative digestibility of food allergens and non-allergenic proteins is crucial when stability to digestion is to be used as a criterion to assess the allergenic potential of novel proteins. Preheating effect on in vitro digestibility has not been fully examined. In this study we investigated the preheating effect of in vitro digestibility of several proteins and their proteolytic fragments in simulated gastric fluid (SGF) and simulated intestinal fluid (SIF). Five major food allergens, ovalbumin (OVA), ovomucoid (OVM), beta-lactoglobulin (BLG), bovine serum albumin (BSA), soybean trypsin inhibitor (STI), four proteins of unproven allergenicity, horseradish peroxidase (HRP), ribulose-1,5-bisphosphate carboxylase/oxidase (RBC), phosphinothricin acetyltransferase (PAT) and zein from corn, and plant lectin, concanavalin A (Con A) were preheated (at 100 degrees C for 5 min) or not preheated, and then digested in SGF or SIF. Food allergens were relatively stable in both SGF and SIF. Among the allergens, digestibility of OVA in both SGF and SIF was markedly decreased, and BLG and STI were relatively stable after preheating. Digestibility of ConA in SGF and SIF was markedly decreased by preheating. Digestibility of non-allergenic proteins in SGF was higher than the allergenic proteins. From these results, because of the marked increase of the digestibility in several proteins by preheating, systematic information concerning the effect of food treatment on protein digestion is necessary to assess the relationship between allergenic potential and the digestibility of food protein.