Nanofibrillar Peptide Hydrogels for the Immobilization of Biocatalysts for Chemical Transformations. Issue 9 (7th March 2014)

• Record Type: Journal Article
• Authors: Hickling, Christopher; Toogood, Helen S.; Saiani, Alberto; Scrutton, Nigel S.; Miller, Aline F.
• Is Part Of: Macromolecular rapid communications. Volume 35:Issue 9(2014:May)
• Page Start: 868
• Page End: 874
• Publication Date: 2014-03-07
• Subjects: Macromolecules -- Periodicals; Polymers -- Periodicals; Chemistry -- Periodicals; 547.705
• DOI: 10.1002/marc.201400027
• Languages: English
• ISSNs: 1022-1336

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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). <boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg5nq92k9c" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>