Covalent immobilization of redox enzyme on electrospun nonwoven poly(acrylonitrile-co-acrylic acid) nanofiber mesh filled with carbon nanotubes: a comprehensive study.
In this work, novel conductive composite nanofiber mesh possessing reactive groups was electrospun from solutions containing poly(acrylonitrile-co-acrylic acid) (PANCAA) and multi-walled carbon nanotubes (MWCNTs) for redoxase immobilization, assuming that the incorporated MWCNTs could behave as electrons transferor during enzyme catalysis. The covalent immobilization of catalase from bovine liver on the neat PANCAA nanofiber mesh or the composite one was processed in the presence of EDC/NHS. Results indicated that both the amount and activity retention of bound catalase on the composite nanofiber mesh were higher than those on the neat PANCAA nanofiber mesh, and the activity increased up to 42%. Kinetic parameters, K(m) and V(max), for the catalases immobilized on the composite nanofiber mesh were lower and higher than those on the neat one, respectively. This enhanced activity might be ascribed to either promoted electron transfer through charge-transfer complexes and the pi system of carbon nanotubes or rendered biocompatibility by modified MWCNTs. Furthermore, the immobilized catalases revealed much more stability after MWCNTs were incorporated into the polymer nanofiber mesh. However, there was no significant difference in optimum pH value and temperature, thermal stability and operational stability between these two immobilized preparations, while the two ones appeared more advantageous than the free in these properties. The effect of MWCNTs incorporation on another redox enzyme, peroxidase, was also studied and it was found that the activity increased by 68% in comparison of composite one with neat preparation.
Wang
Zhen-Gang
ZG
Institute of Polymer Science, and Key Laboratory of Macromolecular Synthesis and Functionalization (Ministry of Education), Zhejiang University, Hangzhou 310027, PR China.
Ke
Bei-Bei
BB
Xu
Zhi-Kang
ZK
D000179:Acrylates / Q000737:chemistry*; D000181:Acrylonitrile / Q000737:chemistry*; D000818:Animals; D002374:Catalase / Q000032:analysis / Q000378:metabolism*; D002417:Cattle; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D005022:Ethyldimethylaminopropyl Carbodiimide / Q000737:chemistry; D008099:Liver / Q000201:enzymology; D008954:Models, Biological; D008970:Molecular Weight; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure; D036103:Nanotechnology / Q000379:methods; D037742:Nanotubes, Carbon / Q000737:chemistry* / Q000648:ultrastructure; D010084:Oxidation-Reduction; D011108:Polymers / Q000737:chemistry; D013056:Spectrophotometry, Ultraviolet; D013388:Succinimides / Q000737:chemistry; D013696:Temperature; D014783:Viscosity
D000179:Acrylates; D004800:Enzymes, Immobilized; D037742:Nanotubes, Carbon; D011108:Polymers; D013388:Succinimides; D002374:Catalase; C036658:acrylic acid; C001426:N-hydroxysuccinimide; D000181:Acrylonitrile; D005022:Ethyldimethylaminopropyl Carbodiimide