This study explored, for the first time, the simultaneous dyeing and functionalization of textiles using enzymatically synthesized mixtures of phloridzin and esculin oligomers. Initial screening using multifiber fabric containing diacetate, cotton, polyamide, polyester, polyacrylonitrile, silk, viscose, and wool revealed that the oligomers successfully imparted color and high antioxidant activity to cotton, polyamide, and viscose. These three materials were therefore selected for determination of key process parameters’ influence, including temperature (35 °C and 75 °C), reaction time (6 h and 19 h), and oligomers’ concentration (1.5 and 3.0 mg/mL). Treated fabrics were evaluated for color strength (K/S), antioxidant activity, and prebiotic capacity (in vitro stratum corneum model), with all properties assessed before and after washing. The results showed that several functionalized fabrics retained coloration and functionality after washing, while fabrics functionalized with esculin oligomers’ mixture showed strong prebiotic capacity. Overall, the polyamide that functionalized with 3.0 mg/mL esculin oligomers for 19 h at 35 °C was identified as a promising candidate for reusable colored textiles, including dermatology-oriented garments for sensitive or atopic skin, sportswear, protective workwear, and daily use functional items such as hygienic pads or cloth liners. These findings demonstrate the feasibility of developing textiles with targeted prebiotic functionality.

Laccase is an oxidase of great industrial interest due to its ability to catalyse oxidation processes of phenols and persistent organic pollutants. However, it is susceptible to denaturation at high temperatures, sensitive to pH and in the presence of high concentrations of solvents, which is a problem for industrial use. To solve this problem, this work develops the synthesis in aqueous medium of a new Mn metalloenzyme with laccase oxidase mimetic catalytic activity. To do this, Geobacillus thermocatenulatus lipase (GTL) is used as a "scaffold" enzyme, which is mixed with a manganese salt at 50ºC in an aqueous medium. This produces in situ formation of manganese (IV) oxide nanowires that interact with the enzyme, obtaining the GTL-Mn bionanohybrid. On the other hand, its oxidative activity was evaluated using the ABTS assay, obtaining a catalytic efficiency 300 times greater than the laccase from Trametes versicolor. These new Mn-metalloenzyme turned out to be 2 times more stable at 40 ºC, 3 times more stable in the presence of 10% acetonitrile and 10 times more stable at 20% acetonitrile than laccase Novozym 51003®. Furthermore, the site-selective immobilized GTL-Mn showed much higher stability then the soluble form. Oxidase-like activity of these Mn-metalloenzyme was successfully performed against other substrates such as L-DOPA or phloridzin in oligomerization reactions.