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Sustainable Approach for Cotton Fabric Pretreatment with Immobilized Enzymes

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Abstract

Enzymes are stereospecific, environmentally friendly, and energy-efficient alternatives to chemical treatments in the textile industry. In traditional applications, enzymes are employed to catalyze the process and then drained out on completion of the process. Despite their many potential applications in textiles, enzymes find a limited level of industrial acceptability. Immobilization is a technique for stabilizing enzymes, extending their useful life, and ensuring the long-term viability of their applications through recovery and reuse. In this work, the feasibility of immobilized enzymes for the complete cotton fabric pre-treatment was studied to develop a sustainable way of enzyme application for multiple cycles. Commercial amylase, pectinase and glucose-oxidase enzymes were covalently immobilized on reversibly soluble-insoluble polymer supports (Chitosan & Eudragit S-100) and utilized for the complete pre-treatment of cotton fabric. Methylene blue exhaustion, wax content and tegewa testing confirm the removal of impurities from grey cotton fabric using immobilized enzymes. The equivalent absorbency and whiteness were observed in samples up to three consecutive cycles of immobilized enzyme reuse. Furthermore, the equivalent uniformity, colour yield and fastness ratings after reactive dyeing of these pretreated samples also confirm that the immobilized enzymes can be reused for multiple cycles in comparison to native enzymes for industrial commercialization.

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Authors and Affiliations

  1. Department of Textile Technology, Dr. B R Ambedkar National Institute of Technology, Jalandhar, 144011, India

    Amit Madhu & Jadunandan Chakraborty

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  1. Amit Madhu
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  2. Jadunandan Chakraborty
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Correspondence to Jadunandan Chakraborty.

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Madhu, A., Chakraborty, J. Sustainable Approach for Cotton Fabric Pretreatment with Immobilized Enzymes. Fibers Polym 23, 993–1007 (2022). https://doi.org/10.1007/s12221-022-4193-1

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  • DOI: https://doi.org/10.1007/s12221-022-4193-1

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