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The demand for high protein and plant-based food products is growing, and in this context pulses (peas, chickpeas, lentils, beans) are of increasing interest for both the food industry and for consumers. Increasing the utilization of pulse proteins as food ingredients has the potential to profoundly benefit the environment, global food security, and human health. However, before their extensive utilization as food ingredients, some challenges related to protein quality, functional properties, and processing behavior need to be elucidated. Besides traditional processing using heat treatment, other food processing methods also have potential for the conversion of pulse ingredients into value-added food products. For example, high pressure processing (HPP) may be harnessed for modification of pulse protein structure, function, and digestibility to expand pulse protein applications. This work evaluated the effects of HPP (600 MPa/5C/4 min) and heat treatment (95C/15 minutes) on the structure, function, and digestibility of lentil protein concentrate (LPC), pea protein concentrate (PPC), and faba bean protein concentrate (FPC), at protein concentrations characteristic of protein-fortified beverages (5% w/w) and soft solid foods with a gel structure (15% w/w). HPP- and heat-induced protein structural changes were investigated via differential scanning calorimetry (DSC) and rheological analysis, and surface hydrophobicity measurements. The effect of HPP and heat treatment on protein functionality was characterized by assessing changes in protein solubility, water holding capacity, and emulsifying and foaming properties. Additionally, the effect of HPP and heat treatment on pulse protein concentrate digestibility was assessed using static or dynamic (TIM-1) in vitro systems. Digesta were analyzed by SDS-PAGE for hydrolyzed band patterns, and the concentration of proteins, peptides of various sizes, and free amino acids was determined using the bicinchoninic acid (BCA) and the o-phthaldialdehyde (OPA) protein assays. The effect of HPP and heat treatment on trypsin inhibitor activity was determined by measuring changes in trypsin activity using N-Benzoyl-DL-arginine 4-nitroanilide hydrochloride (BAPNA) substrate. HPP and heat treatments denatured the pulse proteins and significantly increased their surface hydrophobicity (p