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<0.05). At high protein concentrations, strong gel networks formed upon HPP and heat treatment. Heat treatment resulted in significantly greater gel strength, expressed by the elastic modulus G’, than HPP treatment for all samples (p<0.05). HPP and heat treatments significantly increased water holding capacity in 15% protein gelled samples, but significantly decreased protein solubility in 5% protein solutions (p<0.05). The emulsifying activity of proteins in the 5% protein LPC and PPC significantly decreased after both treatments (p<0.05). However, HPP treatment significantly increased emulsifying stability for 5% protein PPC and FPC, as well as foam expansion and foam liquid stability for 5% protein LPC and PPC (p<0.05). Heat treatment significantly increased foam expansion for 5% protein LPC and FPC, and significantly increased foam liquid stability and emulsifying stability (or produced minimal phase separation) for all protein types (p<0.05). HPP and heat treatments did not impact overall protein digestibility for LPC, PPC, and FPC protein by the completion of static and dynamic in vitro digestion. SDS-PAGE revealed treatment-dependent hydrolyzed peptide patterns in the static gastric digesta of all pulse protein concentrates. HPP-treated PPC underwent a significantly greater degree of proteolysis (p<0.05) during static gastric digestion compared to the untreated and heat-treated PPC samples, for both the 5% and 15% protein systems. HPP-induced gels for the 15% protein LPC and FPC had comparable or greater static gastric in vitro digestibility than their untreated counterparts. Pressure-induced gel structures were also more accessible to gastric proteolysis than heat-induced gels, for both LPC and FPC. Nonetheless, treatment-driven differences in protein digestibility during dynamic digestion were only statistically significant (p<0.05) in the first 20 min of jejunal, ileal, and total digestion for the 5% protein PPC, and the first 60 min of ileal digestion for the 15% protein PPC. Digestibility of PPC starch was also not significantly affected by either of these treatments. Additionally, HPP did not inactivate trypsin inhibitors in PPC, but partially inactivated trypsin inhibitors in LPC and FPC. On the other hand, heat treatment lowered trypsin inhibitor activity by ~69-86%, depending on the protein type. This work demonstrates that both heat treatment and HPP can induce desirable structural and functional changes to pulse protein structure, with HPP having the advantage of better preserving overall product quality and organoleptic properties when used in food applications. HPP-induced structural modification of pulse proteins may even enhance gastric proteolysis, which can have some health benefits in certain consumers, but this issue needs further investigation. Overall, the findings of this work can assist in the development of new pulse protein-based product innovations by using heat or HPP treatments to achieve desirable structure and functional attributes.