Sequential Inkjet Printing of Lysozyme and Tyrosinase on Polyamide Fabric: Sustainable Enzyme Binding on Textile Surface

Abstract

has been covalently bound on various fibrous materials, for example, cotton, [7] polyester (PET), [8] polyamide-6,6 (PA), [9] and wool, [10] but mostly using harsh surface binding chemicals such as glutaraldehyde. Most of these studies involved dipping the fabrics in enzyme containing solutions and lengthy incubating procedures. Amount of enzyme loading and deposition manner was less controllable. A better approach would be free from the use of harsh chemicals, minimize enzyme waste and processing time, ensure more process control, and flexibility. Lysozyme contains three tyrosine residues which tyrosinase can catalyze to covalently bind on a fibrous surface containing amino group. To the best of our knowledge, this unique approach has not been studied prior to this work, specially involving inkjet printing these two enzymes in same process. Inkjet technology ensures direct and precise deposition of biomaterials with highresolution designs for more resource efficient and flexible-scale production compared to conventional approaches, for example, screen printing and coating. However, there are fundamental differences between the working principles and manner of enzyme deposition between these technologies, thus the obtained results might not be directly comparable.Digital inkjet printing of enzymes on textile surfaces has great potential for applications ranging from bacterial inhibition to controlled drug delivery. [11] Textile surfaces can provide greater surface area for accommodating higher numbers of enzyme, along with a flexible, light-weight, and strong support medium, compared to flat film-like surfaces. Textiles made of synthetic fibers are of high industrial interest due to their physical strength, chemical inertness, recyclability, reusability, and applicability in various fields. [12] Several enzymes have been studied to include in an ink solution and optimize their activity after printing. [13] Synthetic textiles have been modified using several pretreatment techniques [14,15] to ensure proper ink adhesion, enzyme adsorption, and activity retention.Plasma pretreatment of PET and PA fabrics was found to be beneficial for inkjet printing of enzymes, replacing the needs of harsh chemical based pretreatment processes. [16][17][18][19] Plasma treatment of PA can modify its topography, increase surface energy, and introduce new functional groups. [20][21][22] Such modification can promote better adsorption of printed enzymes through their amino end groups. [23] However, a considerable amount of enzymes were rinsed away from printed fabrics An ink containing tyrosinase catalyzes the tyrosine residues on lysozyme protein to bind it on a plasma-treated polyamide-6,6 (PA) fabric. Inkjet printing enables controlled and sequential deposition of two enzymes on PA which is necessary for proper binding. The effect of different printing sequences on crosslinking stability and enzymatic activity is presented. The lysozyme bound on the fabric shows satisfactory antimicrobial activity. The printed fabric retains about 6...

Combination of Enzymes with Materials to Give Them Antimicrobial Features: Modern Trends and Perspectives

“…The analysis of current trends in the functionalization of various materials due to the introduction of different enzymes in them ( Table 1 [ 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 ], Figure 1 ) allows us to make several generalizations at the initial stage at once. First of all, this concerns the enzymes used.…”

“…First of all, this concerns the enzymes used. Their diversity is not too wide; mainly these are enzymes that belong to the class of oxidoreductases [ 16 , 17 , 18 , 19 , 20 , 28 , 35 , 36 ] and hydrolases [ 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 37 , 38 , 39 , 40 , 41 ]. Peptidases [ 21 , 31 , 34 , 38 ], various carbohydrases [ 22 , 23 , 24 , 25 , 26 , 27 , 29 , 30 , 32 , 33 , 34 , 39 , 40 ], and esterases [ 37 , 41 ] are actively used among hydrolases for obtaining materials with antimicrobial properties ( Figure 1 ).…”

“…The main action of the used enzymes is aimed at inhibiting cell growth, assembling their structural elements, primarily the cell wall, as well as neutralizing the actions of the Quorum Sensing (QS)-signaling molecules of cells, which mainly transfer bacteria to the status of high resistance to the effects of antimicrobial agents [ 16 , 17 , 18 , 19 , 20 , 24 , 25 , 26 , 30 , 37 , 41 ].…”

“…Firstly, concerns on the use of enzymes capable of generating products that have the potential to suppress the growth of microbial cells since they are effective oxidants (as in the case of H 2 O 2 ) or substances that change the acidity of the media (as in the case of organic acids, in particular, gluconic acid) in the environment of treated cells. Secondly, the catalytic action of enzymes can be combined with the antimicrobial action of antibiotics [ 30 , 31 , 32 , 33 , 34 ], nanoparticles exhibiting an antimicrobial effect [ 37 , 39 , 40 , 41 ], with antimicrobial peptides [ 36 , 37 , 38 ] and with other enzymes [ 25 , 26 , 27 , 28 , 29 ]. Enzymes that exhibit multiple catalytic activities, such as ficin, which, being a sulfhydryl protease, demonstrates peroxidase-like activity [ 34 ], are of the greatest interest.…”

“…It is interesting to note that among the targets for the effects of materials functionalized by enzymes, there are both Gram-positive [ 16 , 17 , 18 , 20 , 23 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 34 , 35 , 37 , 39 , 40 , 41 ] and Gram-negative [ 16 , 17 , 18 , 19 , 21 , 22 , 23 , 24 , 26 , 31 , 32 , 33 , 35 , 36 , 37 , 38 , 39 , 40 , 41 ] bacteria, as well as yeast cells mainly of the genus Candida [ 26 , 28 ].…”