Change search
ReferencesLink to record
Permanent link

Direct link
Rational Design of Spider Silk Materials Genetically Fused with an Enzyme
KTH, School of Biotechnology (BIO), Protein Technology. Swedish University of Agricultural Sciences, Sweden.ORCID iD: 0000-0003-0140-419X
2015 (English)In: Advanced Functional Materials, ISSN 1616-301X, E-ISSN 1616-3028, Vol. 25, no 33, 5343-5352 p.Article in journal (Refereed) Published
Abstract [en]

Enzyme immobilization is an attractive route for achieving catalytically functional surfaces suitable for both continuous and repeated use. Herein, genetic engineering is used to combine the catalytic ability of a xylanase with the self-assembly properties of recombinant spider silk, realizing silk materials with enzymatic activity. Under near-physiological conditions, soluble xylanase-silk fusion proteins assembled into fibers displaying catalytic activity. Also, a xylanase-silk protein variant with the silk part miniaturized to contain only the C-terminal domain of the silk protein formed fibers with catalytic activity. The repertoire of xylanase-silk formats is further extended to include 2D surface coatings and 3D foams, also being catalytically active, showing the versatile range of possible silk materials. The stability of the xylanase-silk materials is explored, demonstrating the possibility of storage, reuse, and cleaning with ethanol. Interestingly, fibers can also be stored dried with substantial residual activity after rehydration. Moreover, a continuous enzymatic reaction using xylanase-silk is demonstrated, making enzymatic batch reactions not the sole possible implementation. The proof-of-concept for recombinantly produced enzyme-silk, herein shown with a xylanase, implies that also other enzymes can be used in similar setups. It is envisioned that the concept of enzyme-silk can find its applicability in, for example, multienzyme reaction systems or biosensors.

Place, publisher, year, edition, pages
Wiley-VCH Verlagsgesellschaft, 2015. Vol. 25, no 33, 5343-5352 p.
Keyword [en]
enzyme immobilization, gene fusion, protein-based materials, recombinant spider silk, xylanase
National Category
Biological Sciences
URN: urn:nbn:se:kth:diva-173964DOI: 10.1002/adfm.201501833ISI: 000360724600012ScopusID: 2-s2.0-84940720206OAI: diva2:859224
Swedish Research Council FormasKnut and Alice Wallenberg Foundation

QC 20151006

Available from: 2015-10-06 Created: 2015-09-24 Last updated: 2015-12-01Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textScopus

Search in DiVA

By author/editor
Hedhammar, My
By organisation
Protein Technology
In the same journal
Advanced Functional Materials
Biological Sciences

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 11 hits
ReferencesLink to record
Permanent link

Direct link