Xylan-Degrading Catalytic Flagellar Nanorods

被引:6
|
作者
Klein, Agnes [1 ]
Szabo, Veronika [1 ]
Kovacs, Matyas [1 ]
Patko, Daniel [3 ]
Toth, Balazs [1 ,2 ]
Vonderviszt, Ferenc [1 ,3 ]
机构
[1] Univ Pannonia, Fac Informat Technol, Res Inst Chem & Proc Engn, Bionanosyst Lab, H-8200 Veszprem, Hungary
[2] Hungarian Acad Sci, Inst Agr, Agr Res Ctr, H-2462 Martonvasar, Hungary
[3] Hungarian Acad Sci, Inst Tech Phys & Mat Sci, Energy Res Ctr, H-1121 Budapest, Hungary
基金
匈牙利科学研究基金会;
关键词
Flagellin; Xylanase A; Polymerization; Self-assembly; Flagellar export; Nanorod; TERMINAL REGIONS; FILAMENT; SECRETION; PROTEINS; ENZYMES; SIGNAL; EXPORT;
D O I
10.1007/s12033-015-9874-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:814 / 819
页数:6
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