Abstract

The plastein reaction was ubiquitously acknowledged for its capacity to enhance the functional properties of protein hydrolysates. Despite this, the specific impact of the plastein reaction on emulsification, a critical functional aspect of protein hydrolysates, remains incompletely understood. In this study, the plastein reaction in silver carp protein hydrolysate (SCPH) was explored. A detailed comparison between the primary product (PP) and the blended product (SCPH–P) in terms of their oil-water interfacial adsorption kinetics and the shear strain of oil-in-water emulsions was reported. The interfacial adsorption kinetics suggested that the higher molecular weight imparted a slow rate of diffusion, penetration, and reorganization to the PP compared to SCPH-P. Furthermore, the elevated surface hydrophobicity also resulted in higher surface activity (i.e., high interfacial pressure) for PP. Simultaneously, nonlinear rheological analysis revealed that PP possessed enhanced resistance to shear strain due to its strong affinity for the oil-water interface of emulsion. These improvements manifested in PP-stabilized emulsions with reduced mean particle size (71.6 μm–9.5 μm), diminished instability index (nearly 3-fold prolongation of stabilization time), and increased electrostatic repulsion (zeta potential values increased from 6-15 mV to 21–27 mV), which underscored a substantial enhancement in the emulsification of SCPH through the plastein reaction. Notably, the emulsifying and rheological properties of PP at a 1% (w/w) concentration were nearly equivalent to those of soybean protein isolate at 0.5% (w/w), highlighting the plastein reaction's innovative potential in utilizing SCPH as a promising emulsifier.

Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call