Relationship between Molecular Structure and Heat-Induced Gel Properties of Duck Myofibrillar Proteins Affected by the Addition of Pea Protein Isolate.

This paper investigates the relationship between the molecular structure and thermally induced gel properties of duck myofibrillar protein isolate (DMPI) as influenced by the addition of pea protein isolate (PPI). The results showed that b* value of the gels increased; however, a* value decreased with the increase of PPI content (p < 0.05). The whiteness of the gels decreased significantly with the addition of pea protein compared with 0% vs. 0.5% addition. Nuclear magnetic resonance tests showed the area of immobilized water also increased with increasing PPI addition (0−2%), thus consistent with the increased water-holding capacity (p < 0.05). The penetration force of the gels increased with increasing PPI addition (p < 0.05), while the storage modulus and loss modulus of the gels were also found to increase, accompanied by the transformation of the α-helix structure into β-sheet, resulting in better dynamics of gel formation. These results indicated the gel-forming ability of DMPI, including water retention and textural properties, improves with increasing PPI addition. Principal component analysis verified these interrelationships. Thus, pea protein could improve the properties of duck myofibrillar protein gels to some extent and improve their microstructure, potentially facilitating the transition from a weak to a non-aggregated, rigid structure.