Fish gelatin has been increasingly used as a safe alternative to cattle and pig gelatin due to its similar structure, avoiding the health and socio-cultural issues associated with the use of materials of mammalian origin. Fish gelatin can be produced from processed fish products to achieve a high yield at a low cost. Recent studies show that although fish gelatin comes from a wide range of sources, the protein content and amino acid composition of fish gelatin from different sources are different, and some fish gelatin is soft and unstable transglutaminase (TGase) can catalyze the γ-amide group of glutamine residues and the ε-amino group of lysine residues in proteins to form covalent bonds to form a stable protein network structure, improve the strength of the gel so that it can be applied in a more special environment. In this experiment, after screening the raw materials of cold-water fish gelatin M06 and M08, warm-water fish gelatin M03 and M04, a strong fish gelatin was successfully prepared by catalytic modification of cold-water fish gelatin by transglutaminase (TGase), and the excellent performance of TG enzyme-catalyzed modified gelatin was proved through the application effect of chicken salt soluble protein. In this experiment, the protein content of cold-water fish M08 was the highest, which was up to 99.9%, 1.09 times that of warm-water fish. The gelatin content of cold-water fish M08 was the highest of the four kinds of fish gelatin, with a wide proportion of components and rich amino acid composition. Cold-water fish M08 gelatin-derived gel had the highest strength of 253 ± 1 g/cm at 4 °C. It was found that fish gelatin with protein molecular weight distribution and rich amino acid composition had higher gel strength. M08 gelatin is cross-linked by transglutaminase (TGase), which increases the strength of enzyme gels by approximately 200% compared to self-assembled gels. Fish gelatin catalyzed by the TG enzyme improves the gel strength of raw material and makes it more applicable. M08 gelatin also showed good application performance at low temperatures in compound chicken salt-soluble protein gel, with a water retention rate of 95.84% and gel strength of 198.5 g/cm. This study expanded the application range of fish gelatin by TG enzyme and improved the application potential of fish gelatin.

Enzymatic additives, particularly alkaline proteases, play a crucial role in enhancing detergent effectiveness against protein-based stains. Despite advancements in enzyme stabilization techniques, there is a need for innovative strategies to further improve protease stability in laundry detergents. However, research exploring the utilization of substrate imprinting technology to achieve this objective remains limited. Therefore, this study aims to enhance the stability of alkaline proteases in laundry detergents by employing casein as an imprinting substrate and utilizing transglutaminase-mediated (TGase) crosslinking to modify proteases 102 and 306. The optimal temperature, pH, and thermal stability of the modified alkaline proteases 102 and 306 showed no significant changes. However, these two modified alkaline proteases exhibited varying degrees of improvement in stability among the 14 detergent additives tested. Under 40 °C incubation for 24 h, the relative enzyme activity of modified alkaline protease 102 increased approximately 1.4–15-fold in AEO-9, BS-12, CMI, APG, FMEE, and SOE, while the relative enzyme activity of modified alkaline protease 306 increased approximately 1.2–3.7-fold across different additives (FMEE, AEO-9, BS-12, SOE, FAA, and AEC-9Na). These modified proteases demonstrated improved stability and wider applicability across commercial detergent formulations available. Integrated into standard laundry detergent at a 1:7 ratio before and after modification, they effectively removed protein stains from the cotton fabric after 24 h of 40 °C incubation. These findings provide insights into more effective stain-removal techniques.

Protease is the main enzyme of detergent. Through the combination of different proteases and the combination of protease and detergent additives, it can adapt to different washing conditions to improve the washing effect. In this experiment, whiteness determination, microscope scanning, Fourier transform infrared spectroscopy, and X-ray photoelectron spectroscopy were used to detect the whiteness values of the cloth pieces before and after washing, as well as the stain residue between the fibers on the surface of the cloth pieces. The protease detergent formula with better decontamination and anti-deposition effects was selected. The combination of alkaline protease, keratinase, and trypsin was cost-effective in removing stains. Polyacrylamide gel electrophoresis showed that the molecular weight of the protein significantly changed after adding the enzyme preparation during washing, and the molecular weight of the protein was directly proportional to protein redeposition. The composite protease had a better comprehensive decontamination effect, and when compatible with suitable surfactants, anti-redeposition agents, and water-softening agents, the compound protease detergent exhibited a stronger decontamination ability than commercial detergents.

Although keratin can effectively repair hair fibres and enhance their moisture content and flexibility, it has a relatively low affinity for hair. In this study, the effects of transglutaminase (TGase)—commonly used to catalyse crosslinking of proteins or amino acids—in crosslinking serine and hydrolysed wool keratin to repair damaged hair and protect healthy hair were studied. Treatment with a repair solution containing hydrolysed wool keratin, serine, and TGase improved the physical and chemical properties of damaged hair samples. The alkali solubility of damaged hair samples decreased by 50.53%, fracture stress increased from 1.031 to 1.806 N, and fracture strain increased from 9.51 to 19.88 mm. Fourier transform infrared spectroscopy and X-ray analysis showed that amide bonds increased in damaged hair samples treated with the repair solution and hair crystallinity increased. Differential scanning calorimetry showed that the repair solution improved the thermal stability of damaged hair. After five cycles of washing, the effects of the repair solution were still apparent in damaged hair samples. The enzymatic solution had stronger repair effects than general hair care products and reduced water loss rates in damaged hair samples; repaired hair samples were also softer and brighter. The repair solution was effective in protecting healthy hair samples against chemical damage. The materials used to prepare the repair solution are all bio-based, and treatment with this product is safer and longer lasting.

Cellulosome is a highly efficient multi-enzyme self-assembly system and is found on the extracellular surface or in the free environment of microorganisms. However, with a lack of Ca²⁺ in vivo, cellulosome assembly is challenging. In this study, a novel design method was used to directionally modify the Ca²⁺-binding site, and four double-site dockerin A (DocA) mutants were obtained. At a Ca²⁺ concentration between 1.00 × 10⁻⁷ and 1.00 × 10⁻⁴ M, the mutant DocA-D3 had the strongest binding capacity to cohesion (Coh), which was 8.01 times that of DocA. The fluorescence signal intensity of the fusion proteins assembled using mutants was up to 1.26 × 10⁷ in Escherichia coli, which indicated that these mutants could interact with Coh in vivo. The molecular dynamics simulation results showed that DocA-D3 could maintain a stable angle structure without Ca²⁺, and when applied to L-lysine fermentation, the yield was increased by 24.1%; when applied to β-alanine fermentation, the product accumulation was increased by 2.13–2.63 times. These findings lay the foundation for assembly design in cells.

Fish gelatin (FG)-based wound dressings exhibit superior water absorption capacity, thermal stability, and gelation properties, which enhance the performance of these dressings. In this study, our objective was to investigate the conditions underlying the enzymatic hydrolysis of FG and subsequent cross-linking to prepare high-performance gels. A two-step enzymatic method of protease-catalyzed hydrolysis followed by glutamine transglutaminase (TGase)-catalyzed cross-linking was used to prepare novel high-performance fish gelatin derivatives with more stable dispersion characteristics than those of natural gelatin derivatives. Compared with conventional TGase cross-linked derivatives, the novel derivatives were characterized by an average pore size of 150 μm and increased water solubility (423.06% to 915.55%), water retention (by 3.6-fold to 43.89%), thermal stability (from 313 °C to 323 °C), and water vapor transmission rate, which reached 486.72 g·m⁻²·24 h⁻¹. In addition, loading glucose oxidase onto the fish gelatin derivatives increased their antibacterial efficacy to >99% against Escherichia coli and Staphylococcus aureus.