Increasing the diversity of nylonases for poly(ester amide) degradation

Author:

de Witt Jan1ORCID,Ostheller Maike-Elisa2,Jensen Kenneth3ORCID,van Slagmaat Christian A. M. R.4ORCID,Polen Tino1ORCID,Seide Gunnar2,Thies Stephan1ORCID,Wynands Benedikt1ORCID,Wierckx Nick1ORCID

Affiliation:

1. Institute of Bio- and Geosciences IBG-1: Biotechnology, Forschungszentrum Jülich, Jülich, Germany

2. Aachen-Maastricht Institute for Biobased Materials (AMIBM), Maastricht University, Brightlands Chemelot Campus, Urmonderbaan 22, 6167 RD Geleen, The Netherlands

3. Novonesis A/S, Biologiens Vej 2, Kgs. Lyngby DK-2800, Denmark

4. B4Plastics BV, IQ-parklaan 2A, 3650, Dilsen-Stokkem, Belgium

Abstract

This study extents the sequence space of 6-aminohexanoate endohydrolases (NylC) for future enzyme engineering strategies to boost their nylonase activities, while in parallel novel polymers were designed to align biodegradability and performance.

Funder

Bio-Based Industries Joint Undertaking

Publisher

Royal Society of Chemistry (RSC)

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