The functional attributes of protein hydrolysates from horsegram ( <i>Macrotyloma uniflorum</i> )

Abstract The functional attributes of enzymatically derived horsegram protein hydrolysates from dehulled horsegram were investigated in this study. Hydrolysates were produced using commercial proteases, namely Alcalase® 2.4L and Protex 6L, at varying degrees of hydrolysis (DH) – specifically, 5%, 8%, and 10%. Maximum DH reached 11% with Alcalase® 2.4L and 11.5% with Protex 6L. Optimal hydrolysis conditions entailed a dehulled horsegram concentration of 2.5% (w/v), an enzyme–substrate ratio (E/S) of 0.001% for Alcalase® 2.4L and 0.002% for Protex 6L, at 55 °C and 60 °C, respectively, for 5 h, maintaining a pH of 7.5. Enhanced solubility was observed across a wide pH range (2–10), with HG-PH exhibiting an increase from 21% to 56%. Analysis of functional properties revealed a significant elevation (P &amp;lt; 0.05) in both water holding and oil holding capacities with increasing DH. Emulsion activity decreased from 0.5 to 0.1 in proportion to DH increase. Conversely, foaming capacity (FC) showed a positive correlation with the hydrolysis extent, rising from 24% to 98%. However, foam stability decreased across all samples, declining from 84% to 12%. These findings underscore the potential of incorporating these hydrolysates into diverse food applications, capitalising on their heightened solubility, water and oil holding capacities, and foam-forming characteristics. The comprehensive array of functional properties exhibited by HG-PH renders it a promising ingredient for integration into food product formulations.