# High Hydrostatic Pressure‐Induced Changes in Carioca Bean Protein: Structural and Techno‐Functional Insights

## TL;DR

This study explores how high pressure affects the structure and functionality of Carioca bean protein, showing improved properties for food applications.

## Contribution

The novel contribution is demonstrating how high hydrostatic pressure modifies Carioca bean protein for better use in plant-based foods.

## Key findings

- High pressure at 600 MPa increases surface hydrophobicity and improves foaming properties of Carioca bean protein.
- Carioca bean protein treated at 600 MPa shows enhanced emulsion stability compared to other pulse proteins.
- Pressure treatment alters particle size and aggregation, impacting techno-functional properties.

## Abstract

Carioca bean protein concentrate (CBPC) has become a noteworthy alternative in the food industry. To expand their utilization in plant‐based food products, this study examined the effects of high hydrostatic pressure (HHP) treatment at 200–600 MPa for 10 min on the structural, techno‐functional, and color properties of CBPC. HHP treatment significantly influenced the structural and techno‐functional properties of CBPC. Particle size increased with pressure, reaching the largest volume‐weighted mean diameter (29.2 µm) at 400 MPa, accompanied by the lowest zeta potential (34.6 mV), indicative of protein aggregation. At 600 MPa, the pressure‐induced breakdown of aggregates resulted in a reduced particle size (14.7 µm) and enhanced exposure of hydrophobic groups. The surface hydrophobicity (H
0) was significantly higher at 600 MPa, leading to increased enthalpy (3.4 J/g) and intrinsic fluorescence. Foaming properties were notably improved at 600 MPa, with an increase in foam capacity (35%) and foam stability (8%). Conversely, treatment at 200 MPa resulted in lower H
0 values, associated with higher protein aggregation and reduced solubility (59%) compared to higher pressure treatments (64%–70%). HHP treatment, particularly at 600 MPa, effectively modifies the structural and functional properties of CBPC, enhancing its potential for use in aerated or foamed food products. Overall, almost all CBPC samples demonstrated emulsion stability close to 100%, surpassing widely used pulse proteins in the food industry. These findings support the use of HHP‐treated CBPC as a versatile ingredient in plant‐based food applications.