The physicochemical and functional attributes of edible dock proteins concentrates.

Amidst rapid global population growth and associated increasing protein deficits, the development of novel protein resources has become imperative. This study investigates the techno-functional properties of Edible dock proteins concentrates (EDP) under varying pH conditions to assess its potential as a functional food ingredient. EDP possesses an excellently balanced amino acid composition, with solubility exceeding 97 % at pH ≥7 and a minimum of 13 % at pH 5. Structural characterization revealed that EDP exhibited a significantly higher α-helix/β-sheet ratio (1.50-1.59) compared to soy protein isolate (SPI, 0.67-0.75) and pea protein isolate (PPI, 0.55-0.76) at pH ≥7. Additionally, EDP showed greater free sulfhydryl content than these counterparts across the studied pH range (5-9). Notably, EDP demonstrated pH-dependent emulsifying capacity (EC, 13.91-40.16 %) and stability (ES, 45.13-57.56 %) at pH 5-9, both of which surpassed SPI and PPI. The α-helix/β-sheet ratio was identified as a key structural parameter associated with excellent EC at pH ≥7, enabling α-helix-dominated interfacial adsorption, ordered molecular alignment at oil-water interfaces, and effective interfacial tension reduction. In contrast, free sulfhydryl content predominantly governed EC at pH 5, where sulfhydryl flexibility facilitated protein unfolding and crosslinking. Multivariate analyses (principal component analysis, PCA, and cluster analysis) further indicated that emulsification performance of the EDP at pH ≥7 was comparable to whey protein isolate (WPI). The combination of superior emulsification properties, advantageous structural characteristics, and high nutritional value establishes EDP as a structurally unique and nutritionally complete sustainable protein source.