Nanofibrillar peptide hydrogels for the immobilization of biocatalysts for chemical transformations

Christopher Hickling, Helen Toogood, Alberto Saiani, Nigel S. Scrutton, Aline Miller

Research output: Contribution to journalArticlepeer-review


Enzymes are attractive, "green" alternatives to chemical catalysts within the industrial sector, but their robustness to environmental conditions needs optimizing. Here, an enzyme is tagged chemically and recombinantly with a self-assembling peptide that allows the conjugate to spontaneously assemble with pure peptide to form β-sheet-rich nanofibers decorated with tethered enzyme. Above a critical concentration, these fibers entangle and form a 3D hydrogel. The immobilized enzyme catalyzes chemical transformations and critically its stability is increased significantly where it retains activity after exposure to high temperatures (90 °C) and long storage times (up to 12 months). Peptide-enzyme conjugates are incorporated within self-assembling peptide fibrillar hydrogels to immobilize the enzyme on the surface of the fibers. Once here, they are capable of catalyzing chemical transformations with increased stability and robustness to storage time and temperature. © 2014 The Authors. Published by WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Original languageEnglish
Pages (from-to)868–874
Number of pages7
JournalMacromolecular rapid communications
Issue number9
Publication statusPublished - May 2014


  • biocatalysis
  • chemical transformation
  • peptide hydrogel
  • self-assembly


Dive into the research topics of 'Nanofibrillar peptide hydrogels for the immobilization of biocatalysts for chemical transformations'. Together they form a unique fingerprint.

Cite this