Our study aimed to explore the ability of extruded maize starch-chlorogenic acid (EMS-CHA) complexes to regulate blood glucose homeostasis. Extrusion processing was used to successfully prepare EMS-CHA complexes, accompanied by a structural transformation of starch from A-type to A+V-type semi-crystalline form. Notably, when chlorogenic acid (CHA) was incorporated at 2.0% (w/w) into maize starch (EMS-2.0CHA), the resistant starch content significantly increased to 30.35 ± 2.36%. This directly contributed to a reduced glycemic response, as evidenced by a lower postprandial blood glucose area under the curve (AUC) of 5.72 ± 1.13 mmol/h·L. The hypoglycemic effect of EMS-2.0CHA complex was further validated in diabetic rats. Compared with high-fat diet group, supplementation with EMS-2.0CHA complex significantly decreased fasting blood glucose levels to 11.75 ± 2.75 mmol/L and reduced the AUC to 15.15 ± 2.63 mmol/h·L. Importantly, these improvements were associated to enhanced pancreatic function: increasing insulin secretion, improving pancreatic mass and reduced apoptosis, thereby ameliorating insulin resistance. These findings initially clarify the mechanism by which dietary extruded maize starch-chlorogenic acid complexes alleviated insulin resistance and provided a better understanding of the influence of chlorogenic acid on starch that promotes body blood glucose homeostasis.

Ganoderma sinense is a traditional and protein-rich edible fungus with outstanding immunoregulatory activity. However, the mechanism through which G. sinense protein hydrolysates and peptides exert their immunomodulatory effects is unclear. The objective of this study was to prepare and isolate immunologically active peptides from G. sinense protein hydrolysates (GSP) and to investigate their impact on the activation of macrophages. G. sinense peptides with low molecular weights (< 1 kDa, 87.76%) markedly promoted RAW264.7 cell proliferation; increased their phagocytic capacity, nitric oxide (NO), tumor necrosis factor-α (TNF-α), interleukin-10 (IL-10), and IL-6 secretion and reactive oxygen species (ROS) production; and upregulated Tlr2 mRNA expression. In addition, GSP promoted nuclear factor kappa-B (NF-κB) activation and translocation through the upregulation of p65 and p-p65 protein expression. Virtual molecular screening technology revealed that compared with other peptides, the SFAGNIPVNR, YGDAFIR and TVSYLPAPQR peptides derived from GSP showed stronger binding affinities. Interaction site map analysis indicated that the SFAGNIPVNR and YGDAFIR peptides formed stable hydrogen bonds with toll-like receptor 2 (TLR2). Together, these results suggested that G. sinense peptides can serve as important ingredients in nutraceuticals or functional foods.

This study investigates the antioxidant and anti-aging properties of Katsuwonus pelamis peptides (KPPs) using a high-fat diet (HFD) Drosophila melanogaster model. In vitro analysis revealed KPPs exhibit potent radical scavenging activity (e.g., DPPH IC₅₀ = 1.80 mg/mL). In HFD-fed flies, KPPs supplementation significantly extended median lifespan by 23.4% (P < 0.01) and improved motor function (e.g., climbing index increased by 30.0%). In the model, KPPs significantly prolonged lifespan, improved motor function, lowered peroxide, malondialdehyde (MDA) levels, and triglyceride content. Concurrently, KPPs enhanced antioxidant enzyme activity, increasing T-SOD by 20.9% and GSH-Px by 80.1%. Furthermore, KPPs attenuated aging by upregulating key antioxidant genes (Sod1, Cat) and inhibiting the insulin/IGF-like signaling (IIS) pathway. KPPs also demonstrated significant intestinal protection: reducing lipid droplet accumulation and ROS levels, decreasing apoptosis in epithelial cells by 43.2%, while suppressing intestinal stem cell proliferation. These effects collectively preserved gut integrity, maintained homeostasis, and contributed to delayed aging. This study provides compelling evidence for KPPs as a novel intervention to counteract HFD-induced damage and mitigate aging processes.

There has been controversy regarding the optimal processing technology that destroys the special spore wall of Ganoderma lucidum so that the functional activity of the internal polysaccharides can be maintained in the most primitive state. Here, high-purity spore polysaccharides derived from the same variety were obtained respectively by three maturation methods, including enzymatic (EW-IB), laser (LW-IB) and mechanical (MW-IB).Structural characterization showed that EW-IB mildly increased the branching degree (0.523) while preserving →3)-β-D-Glcp-(1→; LW-IB slightly reduced it (0.464) without disrupting the main chain glycosidic bonds; MW-IB partially cleaved →6)-β-D-Glcp-(1→ and moderately decreased the branching degree (0.21). Functionally, the experimental results of the LPS-induced inflammation model revealed that the obtained three polysaccharides exerted their regulatory effects by applying differential forces to specific binding sites in the cell. Remarkably, preservation of →3)-β-D-Glcp-(1→ and moderate branching degree correlated with immunomodulatory activity, while excessive glycosidic bond cleavage (MW-IB) or increased branching degree (EW-IB) slightly reduced regulation of inflammatory factors NO and IL-1β. Overall, our findings point towards a valuable approach for the high-value processing and utilization of medicinal fungal polysaccharides.

For the purse of investigating animal derived ingredients in meat products in order to help in identifying adulteration in meat products, optical gene thin-film biosensor chip technology was used to screen and analyze the animal derived components of 23 samples of meat floss, sausage, meat roll, pre-processed meat and dried meat sold on the market. The obtained results were consistent with those of real-time fluorescent quantitative polymerase chain reaction (RT-qPCR). The biosensor chip enabled more efficient screening of unknown samples. When random samples were analyzed using the biosensor chip, the results for 21.7% of these samples were inconsistent with the label information, so adulteration and false labeling of meat products should not be ignored.

Pseudomonas aeruginosa, recognized for its biofilm production and secretion of virulence factors, posing a severe threat in areas such as clinical infections, food contamination, and marine biofouling. To address this, a new type of zinc-binding peptide (CSSP-Zn) was prepared from crimson snapper scales peptides (CSSP) and goslarite, and its antibacterial and anti-quorum-sensing activities toward P. aeruginosa PAO1 were exploited. Results indicated that CSSP-Zn induced planktonic strain PAO1 membrane injury via inhibiting expression levels of cell integrity genes, targeting microbial-specific membrane constituents, disrupting proton motive force, and causing metabolic disturbances. Meanwhile, CSSP-Zn decreased virulence factors pyocyanin, protease and rhamnolipid secretion, while considerably inhibiting quorum sensing-related genes (las, pqs and rhl) expression and decreasing bacterial abundance and pathogenicity in fish models. Moreover, CSSP-Zn not only effectively hindered biofilm formation but also disassembled preformed ones, thus disrupting biofilm topology. Taken together, utilizing food byproducts to obtain CSSP-Zn could help recycle food resources and provide insight into controlling planktonic and biofilm strain PAO1 contamination.

In order to study the effect of cold chain storage on the structural and functional properties of myofibrillar protein and the chemical interactions of surimi gel, the changes in the functional groups and secondary and tertiary structure of myofibrillar protein and the chemical interactions of surimi gel were investigated as a function of cold chain storage time, and the relationship between chemical interactions and myofibrillar protein was evaluated by principal component analysis (PCA) and correlation analysis. Results showed that the salt-soluble protein content, Ca²⁺-ATPase activity and total sulfhydryl content in surimi gel decreased, while the carbonyl content increased during storage. In addition, the secondary structures of myofibrillar protein transformed from an ordered to a disordered state, and the fluorescence intensity decreased, indicating changes in the polar environment of the protein. These findings demonstrate that the active groups in myofibrillar protein are closely related to the formation of gel chemical forces. Therefore, preventing protein oxidation and freeze denaturation at the initial stage of storage is an effective way to maintain the chemical interactions of surimi gel and the gel characteristics. This study can provide basic theoretical support for the quality maintenance of surimi during cold chain storage.

Surimi-based products (such as fish ball, kamaboko and crabstick) are well accepted by consumers and have broad market prospects owing to their health and nutritional properties and convenience. The surimi-based product is an elastic gel formed based on the gelation properties of myofibrillar protein. The processing procedure includes chopping, heating and exogenous substance addition. Therefore, changes in the structural and functional characteristics of surimi myofibrillar protein under typical processing conditions can affect the quality of surimi-based products. In this article, the quality changes and control methods of surimi myofibrillar protein under the typical processing conditions of physical field (heating and comminution), chemical field (pH and ionic strength) and biological field (enzyme and microorganism) are reviewed, aiming to provide a theoretical basis for further development of the surimi-based product processing industry.

With the improvement of living conditions, people’s eating habits gradually trend to “healthy” development. However, it is difficult to strike a balance between “healthy” and “delicious”. Seasoning is a crucial step during cooking. Saltiness is one of the five basic tastes, and it is produced mainly by adding salt in daily life. Salt plays an important role in human life, but excessive sodium intake can lead to many cardiovascular diseases. Today many health authorities around the world advocate a low-sodium diet. In this context, reducing the amount of salt in foods without affecting their flavor or quality has become a popular research topic. This paper reviews the mechanism of salty taste perception and the current status of salt reduction in foods, with special focuse on salty peptides. The sources, preparation and identification methods, synergistic effect and application prospects of salty peptides are outlined in this paper, so as to provide a basis for the development and application of salty peptides, which will help in advancing the salt reduction campaign.

In order to reduce the amount of added sodium in myofibrillar protein (MP) gel, the effects of partial substitution of different chloride salts (CaCl₂, MgCl₂, and KCl) for NaCl on the gel strength, microstructure, water-holding capacity and rheological properties of MP gel were studied. The underlying mechanism of action of sodium substitutes was elucidated by using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and intrinsic fluorescence spectroscopy as well as measuring surface hydrophobicity and sulfhydryl content. The results showed that KCl was the best substitute for NaCl, followed by CaCl₂, and MgCl₂ was least effective in replacing NaCl. The gel strength of the KCl substitution groups (0.5% KCl + 2.5% NaCl, 1.5% KCl + 1.5% NaCl, and 1.0% KCl + 2.0% NaCl; m/m) was better than that of the control group (3% NaCl), while no significant difference in water-holding capacity was found between the two groups (P > 0.05). The gel strength of the 1.5% CaCl₂ + 1.5% NaCl group decreased significantly (P < 0.05), and the water-holding capacity decreased first and then increased. The gel strength significantly decreased (P < 0.05) and the water-holding capacity increased in the MgCl₂ substitution groups. In terms of rheological properties, the storage modulus (G’) of the KCl substitution groups was significantly higher than that of the control group. Substitution of CaCl₂ and MgCl₂ increased the surface hydrophobicity of MP and decreased the sulfhydryl content. Substitution of CaCl₂, MgCl₂, and KCl resulted in a blue shift in intrinsic fluorescence spectra. At low substitution levels (0.5%), the microstructure of MP gel showed no significant difference from that of the control group. The above results indicate that CaCl₂, MgCl₂ and KCl can be used to partially substitute NaCl in surimi gel products.