This study investigated the impact of different enzymes, including trypsin, papain, and pepsin, on the physiochemical, structural, and techno-functional characteristics of edible bird’s nest protein (EBNP) and its hydrolysate (EBNPH) over a period of 1–4 h. The aim was to determine the optimal hydrolysis conditions for releasing peptides and evaluate their antioxidant activities. It was reported that trypsin produced the highest degree of hydrolysis (DH) value (19.21 %), followed by papain (15.6 %). EBNPH produced using trypsin showed a higher ability to scavenge oxidizing radicals (72.5 ± 0.2 %) compared to papain (63.7 ± 0.3 %) and pepsin (57.5 ± 0.2 %). Additionally, trypsin demonstrated significantly higher ABTS scavenging activities for EBNPH (76.3 ± 0.6 %) than papain (60.0 ± 0.2 %) and pepsin (67.0 ± 0.3 %), indicating that trypsin produced the highest amount of EBNPH with the highest antioxidant activity. Furthermore, spectral analyses by FTIR and X-ray diffraction (XRD) indicated that a higher flexibility and mobility of the secondary structures had occurred in EBNPH. Moreover, SEM images provide convincing evidence that enzymolysis improves and speeds up the breakdown of proteins’ structures. In addition, EBNPH was more susceptible to digestion by pepsin (74.15 %) and papain (67.83 %) than with trypsin, resulting in significantly higher values for the digestibility of EBNPH with trypsin (84.14 %). This indicates that the enzyme modification effectively improved the digestibility of the hydrolysate. Molecular docking research provides a comprehensive explanation of the entire process of the interaction between a glycoprotein and trypsin. The aforementioned localized enzymolysis, thus, might change protein conformation between EBNP or intermolecular interaction between EBNP and EBNPH to enhance functionality and increase food processing capacity.
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