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The aim of this research was to investigate the impact of a diet containing galactooligosaccharide (GOS)-fish peptide (FP) conjugates prepared via Maillard reaction on the colonic fermentation properties and the composition of gut microbiota in Sprague-Dawley rats. The rats were fed the GOS diet, FP diet, GOS and FP mixture (GOS/FP) diet, GOS glycated with FP (80 °C for 120 min, G-GOS/FP) diet, or control (CK) diet for three weeks. Compared to the GOS/FP diet, the G-GOS/FP diet greatly changed the pattern of SCFA production in the hindgut of rats, by increasing the total SCFA (44%), butyrate (55%) and propionate (1.23-fold) levels in the proximal colon, and the butyrate levels (74%) in the distal colon, and decreased the production of ammonia in feces (P < 0.05). The G-GOS/FP altered the colonic microbiota by increasing (P < 0.05) the relative abundance of Anaerovibrio (7.43-fold) and Prevotella-9 (2.47-fold), and by decreasing (P < 0.05) the relative abundance of Alloprevotella (0.57-fold) and Holdemanella (0.64-fold), and showed a similar relative abundance of Bifidobacterium, when compared with GOS/FP. The GOS/FP diet increased the number of Lactobacillus and the intensity of fermentation in the cecum, but the G-GOS/FP diet and GOS diet did not have these effects, showing that the glycation clearly altered the fermentability of the fish peptide. It is concluded that the glycation-induced modification of GOS by mild thermal treatments showed its fermentation persistence in the colon of the host, and improved some prebiotic activities of GOS. These results may provide new strategies for oligosaccharides in combination with peptides to modulate the intestinal environment to promote human health.

Aquatic foods, also known as blue foods, contain a wide range of unique bioactive substances. Among these substances, aquatic foods-derived bioactive peptides exhibit diverse structures and activities, including blood pressure reduction, antibacterial effects, uric acid level reduction, and antioxidant effects. As a result, these peptides show considerable potential for application in functional foods. Existing reviews on aquatic foods-derived bioactive peptides have focused primarily on their functional activities and preparation methods, while neglecting the latest trends in rapid discovery and large-scale production of peptides. Therefore, in addition to summarizing the most recent preparation methods of aquatic foods-derived bioactive peptides, this paper also examines the structure-activity relationships and strategies for large-scale production of active peptides. The use of bioinformatics techniques, such as docking and data mining, can significantly expedite the process of discovering and purifying of aquatic foods-derived bioactive peptides. Furthermore, the precise design and optimization of peptides based on their structure-activity relationships can effectively enhance their activity. Heterologous biosynthesis via the modification of host and target peptides holds promise for enabling large-scale production of these peptides. These methods represent the future direction of research on aquatic foods-derived bioactive peptides. • Bioinformatics accelerates the discovery of aquatic foods derived-active peptides. • Active peptide can be rationally designed based on structure-activity relationship. • Heterologous biosynthesis could facilitate the large-scale preparation of peptides. [ABSTRACT FROM AUTHOR]

• Seven XO inhibitory peptides were screened from shrimp via docking and BLAST. • YNITGW (IC 50 = 9.78 ± 0.13 mM) exhibited the greatest XO inhibitory activity. • Hydrogen bond and π-π stacking played a significant role between peptides with XO. • Insertion of Trp in the middle position of peptide could enhance the activity. Xanthine oxidase (XO) inhibitory peptides are safer than conventional pharmacological therapy in relieving hyperuricemia. However, traditional enzymatic hydrolysis, separation, and purification techniques for bio-active peptide preparation are time-consuming, inefficient, and labor-intensive. In this study, molecular docking and BLAST were used to virtually screen XO inhibitory peptides from whole protein sequences of Pacific white shrimp according to the bio-active peptides database, and the structure of peptides was optimized based on the structure-effective relationship. Seven new XO inhibitory peptides were virtual screened rapidly from Pacific white shrimp, and YNITGW (IC 50 = 9.78 ± 0.13 mM) showed the strongest activity. The results of YNITGW optimization showed that the insertion of Trp residue in the middle position of peptides could effectively enhance the activity. This study revealed that screening and optimizing peptides by molecular docking were a novel and feasible method to obtain bio-active peptides. [ABSTRACT FROM AUTHOR]

• Oyster-derived xanthine oxidase inhibitory peptides were first reported. • Three novel xanthine oxidase inhibitory peptides were obtained. • Reveal the mechanism of action of peptides with xanthine oxidase. • A series of designed xanthine oxidase inhibitory peptides were obtained. • Through rational design, the activity of peptides is greatly improved. Xanthine oxidase (XO) inhibitory peptides are secure and efficient functional food ingredients for treating or alleviating hyperuricemia (HUA). In this study, ultrafiltration and molecular exclusion chromatography were used to separate and purify enzymatic lysate of oyster protein, three novel peptides (ALSGSW, GGYGIF and MAIGLW) with strong XO inhibitory activity were screened by LC-MS/MS identification and molecular docking technology. Then, the mechanism of action between peptides and the XO was revealed by molecular docking technology, and the structure of the peptide was rationally designed on this basis. The results showed that replacing N -terminal Gly of peptide GGYGIF with Trp can significantly improve its XO inhibition rate, and peptides formed by the simple structure amino acid was connected to the aromatic amino acids has preferable inhibitory activity. These results showed that oyster was a good source of XO peptide inhibitors, molecular docking technology was an effective tool for obtaining highly active peptides. [ABSTRACT FROM AUTHOR]