| Literature DB >> 25966869 |
Ágnes Klein1, Veronika Szabó, Mátyás Kovács, Dániel Patkó, Balázs Tóth, Ferenc Vonderviszt.
Abstract
Flagellin, the main component of flagellar filaments, is a protein possessing polymerization ability. In this work, a novel fusion construct of xylanase A from B. subtilis and Salmonella flagellin was created which is applicable to build xylan-degrading catalytic nanorods of high stability. The FliC-XynA chimera when overexpressed in a flagellin deficient Salmonella host strain was secreted into the culture medium by the flagellum-specific export machinery allowing easy purification. Filamentous assemblies displaying high surface density of catalytic sites were produced by ammonium sulfate-induced polymerization. FliC-XynA nanorods were resistant to proteolytic degradation and preserved their enzymatic activity for a long period of time. Furnishing enzymes with self-assembling ability to build catalytic nanorods offers a promising alternative approach to enzyme immobilization onto nanostructured synthetic scaffolds.Entities:
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Year: 2015 PMID: 25966869 DOI: 10.1007/s12033-015-9874-1
Source DB: PubMed Journal: Mol Biotechnol ISSN: 1073-6085 Impact factor: 2.695