Exploring the Model of Cefazolin Released from Jellyfish Gelatin-Based Hydrogels as Affected by Glutaraldehyde.

Due to its excellent biocompatibility and ease of biodegradation, jellyfish gelatin has gained attention as a hydrogel. However, hydrogel produced from jellyfish gelatin has not yet been sufficiently characterized. Therefore, this research aims to produce a jellyfish gelatin-based hydrogel. The gelatin produced from desalted jellyfish by-products varied with the part of the specimen and extraction time. Hydrogels with gelatin: glutaraldehyde ratios of 10:0.25, 10:0.50, and 10:1.00 (v/v) were characterized, and their cefazolin release ability was determined. The optimal conditions for gelatin extraction and chosen for the development of jellyfish hydrogels (JGel) included the use of the umbrella part of desalted jellyfish by-products extracted for 24 h (WU24), which yielded the highest gel strength (460.02 g), viscosity (24.45 cP), gelling temperature (12.70 °C), and melting temperature (22.48 °C). The quantities of collagen alpha-1(XXVIII) chain A, collagen alpha-1(XXI) chain, and collagen alpha-2(IX) chain in WU24 may influence its gel properties. Increasing the glutaraldehyde content in JGel increased the gel fraction by decreasing the space between the protein chains and gel swelling, as glutaraldehyde binds with lateral amino acid residues and produces a stronger network. At 8 h, more than 80% of the cefazolin in JGel (10:0.25) was released, which was higher than that released from bovine hydrogel (52.81%) and fish hydrogel (54.04%). This research is the first report focused on the production of JGel using glutaraldehyde as a cross-linking agent.

Jellyfish protein hydrolysates: Multifunctional bioactivities unveiled in the battle against diabetes, inflammation, and bacterial pathogenesis.

This study investigates the multifunctional bioactivities of pepsin-hydrolyzed jellyfish by-products (Rhopilema hispidum and Lobonema smithii), focusing on their anti-α-glucosidase activity, anti-inflammatory effects, anti-bacterial properties, and ability to inhibit biofilm formation of Staphylococcus aureus. Our findings revealed that jellyfish protein hydrolysates, particularly from Rhopilema hispidum, exhibit significant anti-α-glucosidase activity, surpassing the well-known α-glucosidase inhibitor Acarbose. Furthermore, we demonstrated the anti-inflammatory capabilities of these hydrolysates in suppressing lipopolysaccharide (LPS)-induced nitric oxide production in murine macrophage cells. This effect was dose-dependent and non-cytotoxic, highlighting the hydrolysate potential in treating inflammation-related conditions. Regarding anti-bacterial activity, pepsin-hydrolyzed jellyfish selectively exhibited a potent effect against S. aureus, including Methicillin-susceptible and Methicillin-resistant strains. This activity was evident at minimum inhibitory concentrations (MIC) of 25 µg/mL for S. aureus ATCC10832, while a modest effect was observed against other Gram-positive strains. The hydrolysates effectively delayed bacterial growth dose-dependently, suggesting their use as alternative agents against bacterial infections. Most notably, pepsin-hydrolyzed jellyfish showed significant anti-biofilm activity against S. aureus. The umbrella section hydrolysate of Rhopilema hispidum was particularly effective, reducing biofilm formation through downregulating the icaA gene, crucial for biofilm development. Furthermore, the hydrolysates modulated the expression of the agrA gene, a key regulator in the pathogenesis of S. aureus. In conclusion, pepsin-hydrolyzed jellyfish protein hydrolysates exhibit promising multifunctional bioactivities, including anti-diabetic, anti-inflammatory, antibacterial, and anti-biofilm properties. These findings suggest their potential application in pharmaceutical and nutraceutical fields, particularly in managing diabetic risks, inflammation, bacterial infections, and combating the biofilm-associated pathogenicity of S. aureus.