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Possibilities for recycling cellulases after use in cotton processing

Part I: Effects of end-product inhibition, thermal and mechanical deactivation, and cellulase depletion by adsorption

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Abstract

Preliminary recycling experiments with cellulase enzymes after cotton treatments at 50°C showed that activity remaining in the treatment liquors was reduced by about 80% after five recycling steps. The potential problems of end-product inhibition, thermal and mechanical deactivation, and the loss of some components of the cellulase complex by preferential and or irreversible adsorption to cotton substrates were studied. End-product inhibition studies showed that the build-up of cellobiose and glucose would be expected to cause no more than 40% activity loss after five textile treatment cycles. Thermal and mechanical treatments of cellulases suggested that the enzymes start to be deactivated at 60°C and agitation levels similar to those used in textile processing did not cause significant enzyme deactivation. Analysis of cellulase solutions, by fast protein liquid chromatography, before and after adsorption on cotton fabrics, suggested that the cellobiohydrolase II (Ce16A) content of the cellulase complex was reduced, relative to the other components, by preferential adsorption. This would lead to a marked reduction in activity after several treatment cycles and top-up with pure cellobiohydrolase II would be necessary unless this component is easily recoverable from the treated fabric.

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Authors and Affiliations

  1. Department of Textile Design and Production, De Montfort University, The Gateway Leicester, LE1 9BH, United Kingdom

    Helena Azevedo & David Bishop

  2. Department of Textile Engineering, Minho University, 4800-058, Guimarães, Portugal

    Helena Azevedo & Artur Cavaco-Paulo

Authors
  1. Helena Azevedo
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  2. David Bishop
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  3. Artur Cavaco-Paulo
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Correspondence to Artur Cavaco-Paulo.

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Azevedo, H., Bishop, D. & Cavaco-Paulo, A. Possibilities for recycling cellulases after use in cotton processing. Appl Biochem Biotechnol 101, 61–75 (2002). https://doi.org/10.1385/ABAB:101:1:61

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  • DOI: https://doi.org/10.1385/ABAB:101:1:61

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