Abstract
The effects of high-pressure processing (HPP) and heat treatment on the digestibility of protein and starch in pea protein concentrate (PPC) were investigated. Samples of PPC with 5% (5 P) and 15% (15 P) protein were treated by HPP (600 MPa/5 °C/4 min) or heat (95 °C/15 min) and their in vitro static and dynamic digestibility were compared to untreated controls. HPP-treated PPC underwent a greater degree of proteolysis and showed different peptide patterns after static gastric digestion compared to untreated and heat-treated PPC. Differences in protein digestibility among treatments during dynamic digestion were only significant (p < 0.05) during the first 20 min of jejunal, ileal, and total digestion for 5 P, and during the first 60 min of ileal digestion for 15 P. Neither static nor dynamic starch digestibility were dependent on treatment. HPP did not reduce trypsin inhibitor activity, whereas heat treatment reduced it by ~70%. HPP-induced structural modifications of proteins and starch did not affect their overall in vitro digestibility but enhanced gastric proteolysis.
Highlights
High-pressure processing (HPP) is a nonthermal food processing technology that can be used as an alternative to thermal pasteurization, without the detrimental sensory and nutritional changes to the food matrix induced by heat[1]
Both HPP and heat treatment of proteins induce dissociation of subunits, denaturation, and rearrangement of secondary and tertiary structure, which can result in aggregation and formation of gel networks[1,3]
Detailed information regarding structural changes induced in pea protein concentrate (PPC) by both HPP and heat treatment can be found in previous studies by our group[4,5]
Summary
High-pressure processing (HPP) is a nonthermal food processing technology that can be used as an alternative to thermal pasteurization, without the detrimental sensory and nutritional changes to the food matrix induced by heat[1]. Our group recently showed that pressure treatments induce structural modifications in milk and pea proteins, and a range of structures and textures can be created by controlling the pressure level and protein concentration[4,5,6]. These pressure-induced structural modifications of food biopolymers can alter the accessibility of enzymatic cleavage sites, and their susceptibility for enzymatic hydrolysis[7], which has implications for both the shelf life[8] and digestibility of pressure-treated products. Understanding the impact of HPP on the digestibility and trypsin inhibitor activity of pulse proteins is very important, as this can elucidate the effect of this technology on protein quality
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