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Effects of ink characteristics and piezo-electric inkjetting parameters on lysozyme activity
University of Borås, Faculty of Textiles, Engineering and Business.ORCID iD: 0000-0003-2412-9004
University of Borås, Faculty of Textiles, Engineering and Business.ORCID iD: 0000-0002-1008-1313
University of Borås, Faculty of Textiles, Engineering and Business.ORCID iD: 0000-0002-4369-9304
2019 (English)In: Scientific Reports, E-ISSN 2045-2322, Vol. 9, no 18252Article in journal (Refereed) Published
Sustainable development
According to the author(s), the content of this publication falls within the area of sustainable development.
Abstract [en]

Inkjet printing of enzymes can facilitate many novel applications where a small amount of materials need to be deposited in a precise and flexible manner. However, maintaining the satisfactory activity of inkjet printed enzyme is a challenging task due to the requirements of ink rheology and printhead parameters. Thus to find optimum inkjetting conditions we studied the effects of several ink formulation and jetting parameters on lysozyme activity using a piezoelectric printhead. Within linear activity range of protein concentrations ink containing 50 µg/mL lysozyme showed a satisfactory activity retention of 85%. An acceptable activity of jetted ink was found at pH 6.2 and ionic strength of 0.06 molar. Glycerol was found to be an effective viscosity modifier (10–15 mPa.s), humectant and protein structure stabilizer for the prepared ink. A non-ionic surfactant when used just below critical micelle concentration was found to be favourable for the jetted inks. An increase in activity retention was observed for inks jetted after 24 hours of room temperature incubation. However, no additional activity was seen for inkjetting above the room temperature. Findings of this study would be useful for formulating other protein-based inks and setting their inkjet printing parameters without highly compromising the functionality.

Place, publisher, year, edition, pages
2019. Vol. 9, no 18252
Keywords [en]
biological ink, lysozyme, inkjet printing, piezoelectric
National Category
Textile, Rubber and Polymeric Materials
Research subject
Textiles and Fashion (General)
Identifiers
URN: urn:nbn:se:hb:diva-22771DOI: 10.1038/s41598-019-54723-9ISI: 000501310300001Scopus ID: 2-s2.0-85075948827OAI: oai:DiVA.org:hb-22771DiVA, id: diva2:1391140
Available from: 2020-02-03 Created: 2020-02-03 Last updated: 2023-01-11Bibliographically approved
In thesis
1. Enzyme Printed Fabrics: Bio‐functionalisation of Synthetic Textiles by Digital Inkjet Printing
Open this publication in new window or tab >>Enzyme Printed Fabrics: Bio‐functionalisation of Synthetic Textiles by Digital Inkjet Printing
2022 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

This thesis explores the possibilities of printing enzymes using resource-efficient technologies to promote the binding of other proteins and biomaterials on synthetic textiles. This strategy can be used to develop advanced textiles for applications, for example, in antimicrobial, drug delivery and biosensing. Digital inkjet printing was combined with enzyme technology to ensure minimum use of water, chemicals and energy in textile manufacturing processes.  

Inks containing two enzymes, lysozyme and tyrosinase, were formulated by adjusting several rheological and ionic properties. The activity of these enzymes was optimised while being printed through two different industrial grade piezoelectric printheads. The theoretical printability of the prepared inks was calculated. The effect of printhead temperature and number of printing passes on the activity was evaluated. Polyester (polyethylene terephthalate) and polyamide-6,6 were pre-treated through several techniques to understand their effect on enzyme adhesion, binding and activity retention. Tyrosinase was used to bind lysozyme on plasma activated polyamide-6,6 surface. The effects of printing these two enzymes in various sequences, i.e. tyrosinase before lysozyme and vice-versa on binding stability and activity, were studied. Influence of the printing process on enzyme kinetics was evaluated. Ability to store and reuse printed fabrics was also studied.  

Lysozyme and tyrosinase containing inks showed activity retention of 85% and 60%, respectively. Activity of lysozyme containing ink was optimum at 10–15 mPa.s when glycerol was used as a viscosity modifier. However, the optimum viscosity for tyrosinase containing ink was at 6–9 mPa.s, and carboxymethyl cellulose was found to be the most favourable modifier. For both inks, a surfactant amount below the critical micelle concentration was considered to be the most effective for printing. Among the studied fabric pre-treatment methods (alkaline, cutinase and plasma), it was found that the activity and stability of the enzyme were dependent on the nature of the pretreatment processes, which can be beneficial for different application areas, e.g. drug release and bio-sensing. Upon printing both inks on a plasma treated polyamide-6,6, tyrosinase was able to catalyse lysozyme protein to bind it on fabric. A maximum of 68% lytic activity was retained by lysozyme when it was printed after tyrosinase. This fabric showed inhibition of bacterial growth and retained almost half of its initial activity when cold stored for a month. 

Place, publisher, year, edition, pages
Borås: Högskolan i Borås, 2022
Series
Skrifter från Högskolan i Borås, ISSN 0280-381X ; 135
Keywords
Digital printing, inkjet, enzyme, printhead, rheology, immobilisation, piezoelectric, drop-on-demand, resource-efficient textiles, biological ink, lysozyme, tyrosinase, polyphenol oxidase, polyethylene terephthalate, polyester, polyamide-6, 6, nylon, surface modification, plasma, antimicrobial, antibacterial
National Category
Textile, Rubber and Polymeric Materials
Research subject
Textiles and Fashion (General)
Identifiers
urn:nbn:se:hb:diva-29001 (URN)978-91-89271-87-6 (ISBN)978-91-89271-88-3 (ISBN)
Public defence
2023-02-28, M404, Allégatan 1, Borås, 09:00 (English)
Opponent
Supervisors
Available from: 2023-01-31 Created: 2022-12-01 Last updated: 2023-03-06Bibliographically approved

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Biswas, TuserYu, JunchunNierstrasz, Vincent

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