Comparative effects of high pressure processing and heat treatment on in vitro digestibility of pea protein and starch

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.

Design of a Functional Pea Protein Matrix for Fermented Plant-Based Cheese

The production of a fermented plant-based cheese requires understanding the behavior of the selected raw material prior to fermentation. Raw material processing affects physicochemical properties of plant protein ingredients, and it determines their ability to form fermentation-induced protein gels. Moreover, the addition of oil also influences structure formation and therefore affects gel firmness. This study focuses on identifying and characterizing an optimal pea protein matrix suitable for fermentation-induced plant-based cheese. Stability and gel formation were investigated in pea protein matrices. Pea protein isolate (PPI) emulsions with 10% protein and 0, 5, 10, 15, and 20% olive oil levels were produced and further fermented with a starter culture suitable for plant matrices. Emulsion stability was evaluated through particle size, ζ-potential, and back-scattered light changes over 7 h. Gel hardness and oscillation measurements of the fermented gels were taken after 1 and 7 days of storage under refrigeration. The water-holding capacity of the gels was measured after 7 days of storage and their microstructure was visualized with confocal microscopy. Results indicate that all PPI emulsions were physically stable after 7 h. Indeed, ζ-potential did not change significantly over time in PPI emulsions, a bimodal particle size distribution was observed in all samples, and no significant variation was observed after 7 h in any of the samples. Fermentation time oscillated between 5.5 and 7 h in all samples. Higher oil content led to weaker gels and lower elastic modulus and no significant changes in gel hardness were observed over 7 days of storage under refrigeration in closed containers. Water-holding capacity increased in samples with higher olive oil content. Based on our results, an optimal pea protein matrix for fermentation-induced pea protein gels can be produced with 10% protein content and 10% olive oil levels without compromising gel hardness.

Enzymatic Hydrolysis and Fermentation of Pea Protein Isolate and Its Effects on Antigenic Proteins, Functional Properties, and Sensory Profile

Combinations of enzymatic hydrolysis using different proteolytic enzymes (papain, Esperase®, trypsin) and lactic fermentation with Lactobacillus plantarum were used to alter potential pea allergens, the functional properties and sensory profile of pea protein isolate (PPI). The order in which the treatments were performed had a major impact on the changes in the properties of the pea protein isolate; the highest changes were seen with the combination of fermentation followed by enzymatic hydrolysis. SDS-PAGE, gel filtration, and ELISA results showed changes in the protein molecular weight and a reduced immunogenicity of treated samples. Treated samples showed significantly increased protein solubility at pH 4.5 (31.19–66.55%) and at pH 7.0 (47.37–74.95%), compared to the untreated PPI (6.98% and 40.26%, respectively). The foaming capacity was significantly increased (1190–2575%) compared to the untreated PPI (840%). The treated PPI showed reduced pea characteristic off-flavors, where only the treatment with Esperase® significantly increased the bitterness. The results from this study suggest that the combination of enzymatic hydrolysis and lactic fermentation is a promising method to be used in the food industry to produce pea protein ingredients with higher functionality and a highly neutral taste. A reduced detection signal of polyclonal rabbit anti-pea-antibodies against the processed protein preparations in ELISA furthermore might indicate a decreased immunological reaction after consumption.

Multifaceted functionality of L-arginine in modulating the emulsifying properties of pea protein isolate and the oxidation stability of its emulsions

The effects of L-arginine (Arg) at different concentrations (0%, 0.05%, 0.1%, 0.2%, 0.5% and 1.0%) on the antioxidant activity, structure and emulsifying properties of pea protein isolate (PPI) were explored....