Unknown

Dataset Information

0

Nanofibrillar Peptide hydrogels for the immobilization of biocatalysts for chemical transformations.


ABSTRACT: 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 ?-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).

SUBMITTER: Hickling C 

PROVIDER: S-EPMC4316184 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Nanofibrillar Peptide hydrogels for the immobilization of biocatalysts for chemical transformations.

Hickling Christopher C   Toogood Helen S HS   Saiani Alberto A   Saiani Alberto A   Scrutton Nigel S NS   Miller Aline F AF  

Macromolecular rapid communications 20140307 9


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 chemi  ...[more]

Similar Datasets

| S-EPMC1413619 | biostudies-literature
| S-EPMC7411710 | biostudies-literature
| S-EPMC8154259 | biostudies-literature
| S-EPMC6150727 | biostudies-literature
| S-EPMC6014698 | biostudies-literature
| S-EPMC7049098 | biostudies-literature
| S-EPMC2330262 | biostudies-literature
| S-EPMC3105061 | biostudies-literature
| S-EPMC3508364 | biostudies-literature