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Factors modulating the hydrolysis of Nylon-6,6 by a nylon hydrolase enzyme

Journal Article · · Polymer Chemistry
DOI:https://doi.org/10.1039/D5PY00023H· OSTI ID:2540166
 [1];  [2];  [2];  [3];  [1];  [1];  [4];  [1];  [2];  [1];  [5];  [1];  [4];  [1];  [2]
  1. Chemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA
  2. Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA
  3. University of Tennessee-Oak Ridge Innovation Institute, University of Tennessee, Knoxville, TN 37996, USA
  4. Computational Sciences and Engineering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA
  5. Center for Nanophase Materials Science, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA, Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA

We studied the mechanism of hydrolysis of commercial Nylon-6,6 polymer with a thermostable Nylon hydrolyzing enzyme and identified the substrate characteristics that influence the efficiency and deconstruction product yield.

Sponsoring Organization:
USDOE
Grant/Contract Number:
AC05-00OR22725
OSTI ID:
2540166
Alternate ID(s):
OSTI ID: 3002596
Journal Information:
Polymer Chemistry, Journal Name: Polymer Chemistry Journal Issue: 16 Vol. 16; ISSN PCOHC2; ISSN 1759-9954
Publisher:
Royal Society of Chemistry (RSC)Copyright Statement
Country of Publication:
United Kingdom
Language:
English

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