共 50 条
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
相关论文