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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
Identifiers
URN: urn:nbn:se:kth:diva-173964DOI: 10.1002/adfm.201501833ISI: 000360724600012Scopus ID: 2-s2.0-84940720206OAI: oai:DiVA.org:kth-173964DiVA: diva2:859224
Funder
Swedish Research Council FormasKnut and Alice Wallenberg Foundation
Note

QC 20151006

Available from: 2015-10-06 Created: 2015-09-24 Last updated: 2017-12-01Bibliographically approved

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Hedhammar, My

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