Calcium homeostasis imbalance in the body can lead to a variety of chronic diseases. Supplement efficiency is essential. Peptide calcium chelate, a fourth-generation calcium supplement, offers easy absorption and minimal side effects. Its effectiveness relies on peptide's calcium binding capacity. However, research on amino acid sequences in peptides with high calcium binding capacity (HCBC) is limited, affecting the efficient identification of such peptides. This study used soybean peptides (SP), separated and purified by gel chromatography, to obtain HCBC peptide (137.45 μg mg⁻¹) and normal peptide (≤95.78 μg mg⁻¹). Mass spectrometry identified the sequences of these peptides, and an analysis of the positional distribution of characteristic amino acids followed. Two HCBC peptides with sequences GGDLVS (271.55 μg mg⁻¹) and YEGVIL (272.54 μg mg⁻¹) were discovered. Molecular dynamics showed that when either aspartic acid is located near the N-terminal's middle, or glutamic acid is near the end, or in cases of continuous Asp or Glu, the binding speed, probability, and strength between the peptide and calcium ions are superior compared to those at other locations. The study's goal was to clarify how the positions of characteristic amino acids in peptides affect calcium binding, aiding in developing peptide calcium chelates as a novel calcium supplement.

Yeast protein (YP) is rich in nutrients, but its emulsifying properties, especially emulsifying stability, still need to be improved. In this study, cationic polysaccharide chitosan (CS) and anionic polysaccharide xanthan gum (XG) were selected to enhance the emulsifying properties of protein emulsions. The preparation conditions of the emulsions were optimized by calculating particle size, zeta potential, emulsifying activity index, emulsifying stability index, and emulsifying capacity index, as well as macroscopic observation. The optimized emulsions were characterized using confocal laser scanning microscopy, rheology, Raman spectroscopy, color difference analysis, and storage stability. The results showed that the stability of yeast protein/modified yeast protein–chitosan (YP/EYP–CS) emulsions was better at pH 5.5, with a protein:polysaccharide ratio of 1:1 and an oil phase addition of 40%, while the stability of yeast protein/modified yeast protein–xanthan gum (YP/EYP–XG) emulsions was better at pH 3.5, with a protein:polysaccharide ratio of 1:1 and an oil phase addition of 50%. Further analysis indicated that the emulsions with CS had smaller particle sizes and lower initial viscosities, but more hydrogen bonds and better encapsulation of Monascus pigment (MP), especially the EYP–CS emulsion (81.18%). In contrast, the emulsions with XG had uniform droplet sizes and high thermal stability and exhibited obvious shear thinning behavior with increasing shear rates. The network structure of the emulsions was mainly elastic, and the hydrophobic interaction was stronger. This study provides insights into the utilization of yeast protein in the food industry and the development of emulsification systems.

Microbial transglutaminase (mTG) is most frequently utilized in order to increase the gelling properties of soybean protein isolate (SPI), but there are still some limitations of mTG-based hydrogel fabrication technology. Therefore, we aimed to develop a dual modification technique based on enzyme plus organic acid treatment to fabricate SPI hydrogels with high gel strength and stability. Our results showed that mTG plus glucose-δ-lactone (GDL), lactobionic acid (LBA) or maltobionic acid (MBA) treatment could significantly improve the gel strength, textural properties, and water-holding capacity of SPI hydrogels. Also, the addition of these organic acids remarkably reduced the surface hydrophobicity (H₀) and intrinsic fluorescence as well as increased the storage modulus (G′), loss modulus (G″) values, average particle size, and the absolute value of zeta potential of samples. GDL, LBA, or MBA greatly increased the β-sheet level and decreased the α-helix level in hydrogels, as well as dissociated 11S subunits of SPI into 7S subunits. Notably, covalent interactions, hydrogen bonding, and hydrophobic interactions of three organic acids with SPI, as well as the effects of organic acids on the interactions among the intramolecular and intermolecular forces of SPI molecules, contributed to their promoting effects on the formation of hydrogels. The LF-NMR and SEM analyses confirmed the effects of GDL, LBA, and MBA on converting the free water into immobilized and bound water as well as forming a dense stacked aggregate structure. Therefore, GDL, LBA, and MBA are promising agents to be combined with mTG in the fabrication of SPI hydrogels with high gel strength and stability.

Plant-based meat analogs, particularly those produced by high-moisture extrusion, are prone to quality deterioration during frozen storage due to poor freeze–thaw stability. This study aimed to develop a synergistic stabilization strategy for soy protein isolate (SPI)-based extrudates using glucose oxidase (GO), phytase (PA), and tamarind gum (TG). The effects of individual additives (GO, PA, TG) and their combination (GO + TG) were systematically evaluated over seven freeze–thaw cycles, with a pure soybean-protein meat analog (PSM) as a control. The results showed that repeated freeze–thaw cycles severely degraded the control groups, leading to reduced water-holding capacity (WHC), increased hardness, and color darkening. While all additives mitigated these changes, the GO + TG combination exhibited the most pronounced protective effect, maintaining the highest WHC (0.993 ± 0.000), optimal texture (hardness 66.0 ± 0.0 N, elasticity 3.7 ± 0.0 mm), and minimal color variation. Structural analyses revealed that GO + TG effectively suppressed protein oxidation, minimized sulfhydryl loss, preserved protein secondary and tertiary structures, and inhibited the conversion of immobilized water to free water. The synergistic mechanism is attributed to the formation of a dual-network structure, wherein GO enhances covalent cross-linking and TG provides steric stabilization. This study offers a practical and effective approach for enhancing the freeze–thaw stability of extruded plant-based meat products, with potential industrial applications.

The gonad is one of the major byproducts of sea cucumber. Four novel antioxidant peptides (NPWGQ, PGHPF, VPYPR and ATGPQGPAGQRGPAGPTGPTGPAG) were isolated and identified from sea cucumber gonad proteins through enzymatic hydrolysis and antioxidant activity-guided fractionation, bioinformatics approaches and in silico screening. These peptides demonstrated great free radical (2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2′-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS))-scavenging activity and notable superoxide dismutase (SOD)-activation capacity. Molecular docking and molecular dynamics simulation data suggested that these peptides could form strong binding with SOD through hydrogen bonding, electrostatic interactions, and hydrophobic interactions. Among these peptides, NPWGQ displayed the most potent antioxidant and SOD-activating effects. Through searching known databases, these peptides did not show potential toxicity and are generally considered safe. The present study provides crucial theoretical support for comprehensively utilizing sea cucumber (Holothuroidea) gonad by-products and generating high-value functional food ingredients or dietary supplements.