Junde Chen

The swim bladder of Pangasius bocourti is an underutilized fishery byproduct with high protein content, yet its potential as a source of hypoglycemic peptides has not been systematically investigated. This study aimed to prepare and characterize bioactive peptides from P. bocourti swim bladder (PBSB) through integrated enzymatic hydrolysis optimization, peptidomic analysis, and in vivo evaluation. Five proteases were comparatively assessed, and alkaline protease was identified as the optimal enzyme based on degree of hydrolysis and α‐glucosidase inhibitory activity. Under the optimized conditions (pH 9.5, enzyme dosage 2%, 50°C, 4 h), the obtained peptides (PBSBPs) exhibited notable α‐glucosidase inhibitory activity (67.90% ± 0.26% at 5 mg/mL). Nano‐LC–MS/MS analysis identified 101 peptides, of which 91.09% had molecular weights below 1500 Da. The peptide sequences were enriched in hydrophobic and hypoglycemia‐associated amino acid residues, and 58 peptides were predicted to possess α‐glucosidase inhibitory potential. Furthermore, PBSBPs significantly improved glucose tolerance, reduced serum triglyceride and total cholesterol levels, and alleviated hepatic lipid accumulation and pancreatic islet injury in diabetic mice. This study integrates process optimization, peptide profiling, and biological validation, providing a systematic strategy for the development of functional peptides from aquatic byproducts. These findings highlight the potential application of PBSBPs as natural antidiabetic functional ingredients and contribute to the high‐value utilization of fishery processing byproducts.

Traditional chemical hair dyes are associated with potential health risks, while botanical alternatives are often hampered by poor stability and limited color longevity. In this study, discarded squid ink was used to prepare bionic hair colorants of high performance. By synergizing ultrasound disruption with enzymatic hydrolysis, the crude ink aggregates were transformed into highly uniform squid ink melanin nanoparticles (SIMNPs) with size and zeta potential of ~174 nm and −37.5 mV, respectively. This effectively improved the solubility but reduced the steric limitation of natural melanin. To overcome the weak affinity between melanin and human hair, a biomimetic interface where Fe(III) ions act as supramolecular bridges was further engineered to stably bind the SIMNPs to hair keratin. Under optimized conditions (pH 8.0, 45 °C, and 80 min), the dyed hair achieved a natural deep black with a total color difference (ΔE*) of 68.79 ± 0.29, which was maintained at 63.19 ± 0.27 even after 13 consecutive water washing cycles. Unlike destructive oxidative dyes, this SIMNP dyeing system assisted by coordination-driven assembly preserved the native α-helical architecture and disulfide bond networks of hair keratin. Furthermore, the deposited SIMNP layer effectively protected hair fibers from ultraviolet (UV) damage due to its powerful UV-shielding capacity. Crucially, in vitro and in vivo evaluations confirmed the exceptional biosafety of this formulation, demonstrating robust cellular tolerance and absence of murine skin irritation. The work demonstrates a green, low-damage paradigm for the development of bio-based hair colorants of high performance and presents a promising pathway for the high-value utilization of marine by-products.

Fish-derived collagen can reduce the risk of disease transmission and has no religious or cultural restrictions. However, it has limited applications due to its poor thermal stability. In this study, black carp swim bladder collagen (BBC), classified as a type I collagen, was extracted. Amino acid composition analysis revealed that BBC had a higher proline hydroxylation rate of 39.57%. Fourier transform infrared spectroscopy revealed that BBC exhibited a complete triple-helix structure. The fractional viscosity curve and differential scanning calorimetry curves revealed that the thermal denaturation temperature (Td) and the melting temperature (Tm) were 30.85 °C and 107.19 °C, respectively. The dynamic rheological analysis showed that as the concentration increased from 5 mg/mL to 20 mg/mL at 0.01 Hz, the storage modulus increased from 0.979 Pa to 84.2 Pa. When the temperature exceeded the Td, the BBC solution exhibited viscous behaviour as the frequency increased. The steady-shear analysis showed that the BBC was a shear-thinning fluid. Functional properties analysis revealed that BBC exhibited better emulsification properties, foaming properties, water absorption capacity and oil absorption capacity than land-derived collagen, making it suitable for emulsifiers, bubbling beverages, and frozen meat preservation. Additionally, BBC promoted the growth of MT3C3-E1 cells and maintained the normal morphology of the cells. These results showed that BBC is a promising substitute for terrestrial collagen in functional foods, cosmetics, and biofunctional materials.

This study compared collagens from cold-water and warm-water fish for their structural, rheological, and functional properties, and explored their potential applications, aiming to realize the high-value utilization of marine biological resources. To this end, chum salmon skin collagen (CSSC) and Nile tilapia skin collagen (NTSC) were both successfully extracted. Collagens from the two species had different primary and secondary structures, with NTSC having a higher molecular weight, imino acid content, and α-helices and β-turns content. The denaturation temperatures were 12.01 °C for CSSC and 31.31 °C for NTSC. CSSC was dominated by viscous behavior and its structure varied with temperature, while NTSC was dominated by elastic behavior and its structure remained stable with temperature. Both collagens had good oil holding capacity, foaming capacity, and emulsifying activity, but NTSC had better water holding capacity and foaming and emulsifying stability. Their different properties make CSSC more suitable for the preservation of frozen and chilled foods and the production of sparkling beverages, and give NTSC greater potential in biofunctional materials and solid food processing.

Collagen is an important biopolymer widely used in food, cosmetics and biomedical applications. Understanding the effect of pH on the structure and properties of collagen is beneficial for its further processing and exploitation. In this study, greenfin horse-faced filefish skin collagen (GHSC) was prepared and identified as a type I collagen. We systematically investigated the effect of pH on the structural, functional and rheological properties of GHSC. Scanning electron microscopy showed that the collagen morphology changed from an ordered stacked sheet structure to a rough silk-like structure as pH increased. Gaussian-fitted Fourier infrared spectroscopy results of the collagen revealed that it unfolded with increasing pH. Moreover, the ordered structure was reduced, and random coils became the dominant conformation. Its β-sheet and random coil contents increased from 18.43 ± 0.08 and 33.62 ± 0.17 to 19.72 ± 0.02 and 39.53 ± 1.03%, respectively, with increasing pH. α-helices and β-turns decreased from 35.00 ± 0.26 and 12.95 ± 0.01 to 29.39 ± 0.92 and 11.36 ± 0.10%, respectively. The increase in β-sheets and random coils allowed the pI-treated collagen to exhibit maximum water contact angle. The emulsification and foaming properties decreased and then increased with increasing pH in a V-shape. The increased net surface charge and β-sheets in collagen benefited its emulsification and foaming properties. The rheological results showed that the protoprotein exhibited shear-thinning properties in all pH ranges. The collagen solutions showed liquid-like behaviour in low-pH (2, 4) solutions and solid-like behaviour in high-pH (6, 7.83 and 10) solutions. Moreover, the frequency-dependent properties of the storage modulus (G′) and loss modulus (G″) of the collagen solutions weakened with increasing pH. Collagen has considerable frequency-dependent properties of G′ and G″ at low pH (2, 4). Thus, the importance of collagen raw material preparation for subsequent processing was emphasised, which may provide new insights into applying collagen-based materials in food, biomaterials and tissue engineering.

The objective of this study was to develop aquatic collagen production from fish processing by-product skin as a possible alternative to terrestrial sources. Silver carp skin collagen (SCSC) was isolated and identified as type I collagen, and LC-MS/MS analysis confirmed the SCSC as Hypophthalmichthys molitrix type I collagen, where the yield of SCSC was 40.35 ± 0.63% (dry basis weight). The thermal denaturation temperature (T_d) value of SCSC was 30.37 °C, which was superior to the collagen of deep-sea fish and freshwater fish. Notably, SCSC had higher thermal stability than human placental collagen, and the rheological experiments showed that the SCSC was a shear-thinning pseudoplastic fluid. Moreover, SCSC was functionally superior to some other collagens from terrestrial sources, such as sheep, chicken cartilage, and pig skin collagen. Additionally, SCSC could provide a suitable environment for MC3T3-E1 cell growth and maintain normal cellular morphology. These results indicated that SCSC could be used for further applications in food, cosmetics, and biomedical fields.

Marine collagen is an ideal material for tissue engineering due to its excellent biological properties. However, the limited mechanical properties and poor stability of marine collagen limit its application in tissue engineering. Here, collagen was extracted from the skin of tilapia (Oreochromis nilotica). Collagen-thermoplastic polyurethane (Col-TPU) fibrous membranes were prepared using tilapia collagen as a foundational material, and their physicochemical and biocompatibility were investigated. Fourier transform infrared spectroscopy results showed that thermoplastic polyurethane was successfully combined with collagen, and the triple helix structure of collagen was retained. X-ray diffraction and differential scanning calorimetry results showed relatively good compatibility between collagen and TPU.SEM results showed that the average diameter of the composite nanofiber membrane decreased with increasing thermoplastic polyurethane proportion. The mechanical evaluation and thermogravimetric analysis showed that the thermal stability and tensile properties of Col-TPU fibrous membranes were significantly improved with increasing TPU. Cytotoxicity experiments confirmed that fibrous membranes with different ratios of thermoplastic polyurethane content showed no significant toxicity to fibroblasts; Col-TPU fibrous membranes were conducive to the migration and adhesion of cells. Thus, these Col-TPU composite nanofiber membranes might be used as a potential biomaterial in tissue regeneration.