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In this study, hydrolysates of large yellow croaker (Pseudosciaena crocea) roe were prepared by trypsin (Try‐pcRHs) and papain (Pap‐pcRHs). The degree of hydrolysis (DH), molecular weight distribution and iron chelating capacity of hydrolysates were investigated. Moreover, the chelation mechanism of iron‐hydrolysates complex also was investigated by amino acid composition analysis, fourier transform infrared spectrophotometer, fluorescence spectrophotometer and ultraviolet–visible spectroscopy. These results showed that Try‐pcRHs exhibited higher iron chelating ability with the EC50 value of 0.14 mg/ml than Pap‐pcRHs, which may be due to the higher DH and content of peptide <1 KDa. Furthermore, the Asp, Glu, Ser, Pro, Ile, Phe and His in Try‐pcRHs might contribute to the chelation reaction, and the groups of ‐COOH, C=O, N‐H and C‐O were involved in chealtiong of Try‐pcRHs with iron. Therefore, Try‐pcRHs have the potential to be used as iron supplements in food industries. Practical Applications: Large yellow croaker (Pseudosciaena crocea) roes are the main by‐products in the large yellow croaker processing. Previous studies have found that protein isolates from P. crocea roes composed of vitellogenin B, vitellogenin C and vitellogenin contain a large number of serine residues. In this study, we prepared hydrolysates from large yellow croaker roes, and the results showed that trypsin‐hydrolyzed large yellow croaker roes exhibited great iron‐chelating ability and has the potential to be used as a safe and healthy iron supplements in the food industry. [ABSTRACT FROM AUTHOR]

This study investigated the influence of heat treatment on the interaction of large yellow croaker (Pseudosciaena crocea) roe protein isolate (pcRPI) with curcumin (Cur), and heated pcRPI (HpcRPI)-Cur and pcRPI-Cur complexes were also prepared. Fourier transform infrared spectroscopy, fluorescence spectroscopy, and surface hydrophobicity analysis indicated that pcRPI and HpcRPI bind to Cur mainly by hydrogen bonds, van der Waals forces, and hydrophobic interactions, and compared with pcRPI, HpcRPI showed better binding effects with Cur. Molecular docking analysis also evaluated the binding site and the forces between vitellogenin, vitellogenin B and C in pcRPI and Cur. Furthermore, HpcRPI-Cur could form gels induced by glucono-δ-lactone (GDL), while pcRPI-Cur-GDL exhibited a fluid state. The HpcRPI-Cur-GDL gels showed great protective effects on Cur in the resistant gastrointestinal environment. These results indicated that heat treatment will improve the application of pcRPI as a functional material in the food field. [Display omitted] • The pcRPI can bind to curcumin via noncovalent interactions and form complexes. • The heat treatment promoted the noncovalent interactions of pcRPI with curcumin. • The heat treatment enhanced the formation of pcRPI cold-set gels. • The heated-pcRPI gel significantly improved the delivery effect of curcumin. [ABSTRACT FROM AUTHOR]

In this study, cold-set large yellow croaker (Pseudosciaena crocea) roe protein isolate (pcRPI) gels were prepared by glucono-δ-lactone (GDL) at different concentrations. The 0.1% and 0.2% GDL induced pcRPI at 50 mg/mL to form cold-set gels, while pcRPI suspension with 0.4% GDL addition still showed a fluid state. The pcRPI gel induced by 0.2% GDL showed better rheological properties and its G' value was about 5.1 times than that of 0.1% GDL. In addition, pcRPI gels induced by 0.1% and 0.2% GDL showed similar water holding capacity, and 0.2% GDL-induced pcRPI gels showed a special T 2 peak in 2249.0 ms which might represent free water on the surface of the gel. Furthermore, the higher total number of junctions, vessels percentage area, and lower lacunarity indicated a denser three-dimensional network structure in pcRPI gels induced by 0.1% and 0.2% GDL. Particle size tests and AFM results further confirmed that GDL induced pcRPI to form cold-set gels by promoting the formation of protein aggregates. Therefore, 0.1–0.2% GDL are suitable to prepare pcRPI cold-set gels. These results may deepen the understanding on cold-set pcRPI gels induced by GDL. • Pseudosciaena crocea roe protein isolates (pcRPI) had potential to form cold-set gels. • 0.2% glucono-δ-lactone (GDL)-induced pcRPI gels showed good rheological properties. • The 0.1–0.2% GDL induced pcRPI gels had a dense three-dimensional network structure. • GDL-induced pcRPI gels were promoted by the formation of protein aggregates. [ABSTRACT FROM AUTHOR]

Roes are the main byproducts during the processing of large yellow croaker (Pseudosciaena crocea) and have not been well utilized. Heat-induced gels were prepared by using P. crocea roe protein isolates (pcRPI), and the influence of pH on the gel properties was also investigated. pcRPI could not form a gel at pH 4–6 but showed gelation behaviors at pH 7–9. The pcRPI gels prepared at pH 8 had a lower gel point (84 °C), and their G ′ reached 535.4 Pa. Moreover, pcRPI gels formed at pH 8–9 had a more continuous network structure with a shorter T 2 relaxation time than those at other pH conditions. Additionally, vitellogenin and vitellogenin B and C in pcRPI easily formed protein complexes during heating. The hydrophobic interactions, which were the main force between protein molecules during heating, as shown by molecular dynamics simulation, also contributed to gel formation. pcRPI has the potential to be used as a novel hydrogel product in food and other fields. • The optimum pH of P. crocea roe protein isolates (pcRPI) to form gels was pH 8. • The water holding ability of pcRPI gels was enhanced as pH increased. • The pcRPI gels had smoother surface and continuous network structure at pH 8–9. • Hydrophobic interactions were the main forces in the formation of pcRPI gels. [ABSTRACT FROM AUTHOR]

• Gellan gum (GG) improved gel formation of protein isolate from P. crocea roe (pcRPI). • GG improved the rheological properties and water holding ability of pcRPI gels. • The pcRPI-GG binary gels showed denser, more aggregated network structure. • GG improved the protective effects of curcumin by pcRPI gels with control release. The aim of this study was to investigate the effect of gellan gum (GG) on the cold gelation of large yellow croaker roe protein isolate (pcRPI). The water-holding ability and storage modulus of the pcRPI-GG binary gels increased with the GG concentration, where the storage modulus of the pcRPI-0.2% GG gel was approximately 30.7 times that of the pure pcRPI gel. Compare to the other binary gels, pcRPI-0.2% GG gels exhibited a lower lacunarity and higher junction density, with a denser, more aggregated microstructure. Consequently, curcumin was embedded in pcRPI-0.2% GG gels, and simulated gastrointestinal digestion test results showed that GG addition effectively protected and slowed curcumin release in the gastrointestinal environment. These findings may contribute to elucidating the interaction of pcRPI with GG and demonstrate the potential of binary gels for the embedding and delivery of active substances. [ABSTRACT FROM AUTHOR]