Herein, the microstructure and mechanical properties of hydrogels consisting of unrinsed sturgeon surimi (URSS) and plant-derived polysaccharides such as κ-carrageenan (KC), konjac gum (KG), xanthan gum (XG), guar gum (GG) and sodium alginate (SA), were studied by texture analysis, rheological measurement and scanning electron microscopy (SEM). Rheological results showed that the apparent viscosity, storage modulus (G′) and loss modulus (G″) of URSS increased by addition of KC, KG, GG and SA. The gel strength of resultant surimi products fabricated with KG/URSS mixture was significantly higher than that of other groups. KG could significantly improve the hardness (44.14 ± 1.14 N), chewiness (160.34 ± 8.33 mJ) and cohesiveness (0.56 ± 0.02) of the unrinsed surimi gel. Adding SA and KC had no significant effect on the textural characteristics of printed gels. However, an apparent decrease in the relevant mechanical properties of printed hydrogels was observed when XG and GG were added into surimi. SEM indicated that the incorporation of KG and KC could further integrate the gel structure of URSS as compared to hindering the cross-linking of surimi protein by XG and GG, which were in accordance with gel strength and water-holding capacity. These results provided useful information to regulate the 3D printing performance in functionalized surimi-based material.

Hyperuricemia is linked to a variety of disorders that can have serious consequences for human health. Peptides that inhibit xanthine oxidase (XO) are expected to be a safe and effective functional ingredient for the treatment or relief of hyperuricemia. The goal of this study was to discover whether papain small yellow croaker hydrolysates (SYCHs) have potent xanthine oxidase inhibitory (XOI) activity. The results showed that compared to the XOI activity of SYCHs (IC₅₀ = 33.40 ± 0.26 mg/mL), peptides with a molecular weight (MW) of less than 3 kDa (UF-3) after ultrafiltration (UF) had stronger XOI activity, which was reduced to IC₅₀ = 25.87 ± 0.16 mg/mL (p < 0.05). Two peptides were identified from UF-3 using nano-high-performance liquid chromatography–tandem mass spectrometry. These two peptides were chemically synthesized and tested for XOI activity in vitro. Trp-Asp-Asp-Met-Glu-Lys-Ile-Trp (WDDMEKIW) (p < 0.05) had the stronger XOI activity (IC₅₀ = 3.16 ± 0.03 mM). The XOI activity IC₅₀ of the other peptide, Ala-Pro-Pro-Glu-Arg-Lys-Tyr-Ser-Val-Trp (APPERKYSVW), was 5.86 ± 0.02 mM. According to amino acid sequence results, the peptides contained at least 50% hydrophobic amino acids, which might be responsible for reducing xanthine oxidase (XO) catalytic activity. Furthermore, the inhibition of the peptides (WDDMEKIW and APPERKYSVW) against XO may depend on their binding to the XO active site. According to molecular docking, certain peptides made from small yellow croaker proteins were able to bind to the XO active site through hydrogen bonds and hydrophobic interactions. The results of this work illuminate SYCHs as a promising functional candidate for the prevention of hyperuricemia.