The impact of ultrasound-assisted extraction (UAE) was evaluated on the functionality of jackfruit leaf protein hydrolysates. Leaf protein concentrate was obtained by ultrasound (LPCU) and conventional extractions by maceration (LPCM). LPCM and LPCU were hydrolyzed with pancreatin (180 min), and hydrolysates by maceration (HM) and ultrasound (HU) were obtained. The composition of amino acids, techno-functional (solubility, foaming, and emulsifying properties), and antioxidant properties of the hydrolysates were evaluated. A higher amount of essential amino acids was found in HU, while HM showed a higher content of hydrophobic amino acids. LPCs exhibited low solubility (0.97–2.89%). However, HM (67.8 ± 0.98) and HU (77.39 ± 0.43) reached maximum solubility at pH 6.0. The foaming and emulsifying properties of the hydrolysates were improved when LPC was obtained by UAE. The IC₅₀ of LPCs could not be quantified. However, HU (0.29 ± 0.01 mg/mL) showed lower IC₅₀ than HM (0.32 ± 0.01 mg/mL). The results reflect that the extraction method had a significant (p < 0.05) effect on the functionality of protein hydrolysates. The UAE is a suitable method for enhancing of quality, techno-functionality, and antioxidant properties of LPC.

Jackfruit leaf protein concentrate (LPC) was hydrolyzed by pepsin (H–Pep) and pancreatin (H–Pan) at different hydrolysis times (30–240 min). The effect of the enzyme type and hydrolysis time of the LPC on the amino acid composition, structure, and thermal properties and its relationship with the formation of O/W emulsions were investigated. The highest release of amino acids (AA) occurred at 240 min for both enzymes. H–Pan showed the greatest content of essential and hydrophobic amino acids. Low β-sheet fractions and high β-turn contents had a greater influence on the emulsifier properties. In H–Pep, the β-sheet fraction increased, while in H–Pan it decreased as a function of hydrolysis time. The temperatures of glass transition and decomposition were highest in H–Pep due to the high content of β-sheets. The stabilized emulsions with H–Pan (180 min of hydrolysis) showed homogeneous distributions and smaller particle sizes. The changes in the secondary structure and AA composition of the protein hydrolysates by the effect of enzyme type and hydrolysis time influenced the emulsifying properties. However, further research is needed to explore the use of H–Pan as an alternative to conventional emulsifiers or ingredients in functional foods.