Nanobiocatalysis and its potential applications

Kim, J.B.

doi:10.1016/j.jbiotec.2010.08.185

Cited by 9 publications

(14 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The polymerizing ability of the FliC(XynA) fusion protein was investigated by inducing nucleation and polymerization by ammonium sulfate (AS) [13] . Protein solutions of 1 to 1.5 mg/ml were prepared in 20 mM Tris-HCl (pH 7.8) containing 150 mM NaCl and 4 M AS was added to various final concentrations in the range of 0.4 M to 0.8 M. Filament formation was observed after 24 h of incubation at room temperature.…”

Section: Methodsmentioning

confidence: 99%

Construction of a Xylanase A Variant Capable of Polymerization

et al. 2011

View full text Add to dashboard Cite

The aim of our work is to furnish enzymes with polymerization ability by creating fusion constructs with the polymerizable protein, flagellin, the main component of bacterial flagellar filaments. The D3 domain of flagellin, exposed on the surface of flagellar filaments, is formed by the hypervariable central portion of the polypeptide chain. D3 is not essential for filament formation. The concept in this project is to replace the D3 domain with suitable monomeric enzymes without adversely affecting polymerization ability, and to assemble these chimeric flagellins into tubular nanostructures. To test the feasibility of this approach, xylanase A (XynA) from B. subtilis was chosen as a model enzyme for insertion into the central part of flagellin. With the help of genetic engineering, a fusion construct was created in which the D3 domain was replaced by XynA. The flagellin-XynA chimera exhibited catalytic activity as well as polymerization ability. These results demonstrate that polymerization ability can be introduced into various proteins, and building blocks for rationally designed assembly of filamentous nanostructures can be created.

show abstract

Section: Methodsmentioning

confidence: 99%

Construction of a Xylanase A Variant Capable of Polymerization

et al. 2011

View full text Add to dashboard Cite

show abstract

“…按照酶与纳米载体结合的方式, 固定化方法可分为吸附法、包埋法和共价偶联法三种 [3] . 吸附法是将纳米载体(如纳米颗粒等)与含有所需酶溶液直接混合, 在合适条件下纳米载体可以通过静电等作用将酶分子吸附到纳米载体表面 [3] .…”

Section: 纳米载体固定化酶的类型unclassified

“…按照酶与纳米载体结合的方式, 固定化方法可分为吸附法、包埋法和共价偶联法三种 [3] . 吸附法是将纳米载体(如纳米颗粒等)与含有所需酶溶液直接混合, 在合适条件下纳米载体可以通过静电等作用将酶分子吸附到纳米载体表面 [3] . 包埋法, 顾名思义就是将酶包埋在特定载体中, 如可以将酶与聚合物单体混合, 进而通过单体聚合就可以把酶分子固定到聚合物中 [3] .…”

Section: 纳米载体固定化酶的类型unclassified

“…吸附法是将纳米载体(如纳米颗粒等)与含有所需酶溶液直接混合, 在合适条件下纳米载体可以通过静电等作用将酶分子吸附到纳米载体表面 [3] . 包埋法, 顾名思义就是将酶包埋在特定载体中, 如可以将酶与聚合物单体混合, 进而通过单体聚合就可以把酶分子固定到聚合物中 [3] . 共价结合法是利用酶分子的氨基酸残基所含的氨基、羧基或羟基等官能团, 与纳米载体相互补的官能团之间形成共价键来实现酶的固定化 [3] .…”

Section: 纳米载体固定化酶的类型unclassified

“…包埋法, 顾名思义就是将酶包埋在特定载体中, 如可以将酶与聚合物单体混合, 进而通过单体聚合就可以把酶分子固定到聚合物中 [3] . 共价结合法是利用酶分子的氨基酸残基所含的氨基、羧基或羟基等官能团, 与纳米载体相互补的官能团之间形成共价键来实现酶的固定化 [3] .…”

Section: 纳米载体固定化酶的类型unclassified

See 2 more Smart Citations

Current developments and trends in nanobiocatalysis

Gao¹,

Wei²,

Qu³

2020

Sci. Sin.-Vitae

View full text Add to dashboard Cite

show abstract

Design and preparation of stable CPO/HRP@H‐MOF(Zr) composites for efficient bio‐catalytic degradation of organic toxicants in wastewater

Gao

Zhai

et al. 2018

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

BACKGROUND Immobilization of enzyme on a solid support can improve its stability, however, this is often accompanied by a decrease of the initial catalytic activity. The design and preparation of immobilized enzyme with simultaneous high activity and stability is a challenge. RESULTS A hierarchically porous metal organic framework H‐MOF(Zr) which was prepared by ‘crystal defect’ strategy was very stable in aqueous solution and possessed well‐defined, tunable and adjacent hierarchical pores. When using the H‐MOF(Zr) as support for enzyme immobilization, a single array of enzyme in a single mesoporous channel was achieved so as to avoid aggregation of the enzyme. Meanwhile the micropores can be utilized to concentrate substrates, resulting in a decrease in the mass transfer resistance of substrate compared with that in the bulk buffer due to the enzymes and substrates closely embedded on the same support. The prepared immobilized enzyme CPO/HRP@H‐MOF(Zr) was more stable at elevated temparatures, showing 58.2% enhanced activity compared with free enzymes at 70 °C for 1 h incubation. After 12 cycles, 70.7% of activity remained. When the CPO/HRP@H‐MOF(Zr) was applied in the treatment of wastewater containing isoproturon and 2,4‐dichlorophenol, complete degradation was achieved in only 15 min. CONCLUSION Both high activity and stability under harsh reaction conditions give the CPO/HRP@H‐MOF(Zr) composites potential for practical application in wastewater treatment. © 2018 Society of Chemical Industry

show abstract

Nanobiocatalysis and its potential applications

Cited by 9 publications

References 0 publications

Construction of a Xylanase A Variant Capable of Polymerization

Construction of a Xylanase A Variant Capable of Polymerization

Current developments and trends in nanobiocatalysis

Design and preparation of stable CPO/HRP@H‐MOF(Zr) composites for efficient bio‐catalytic degradation of organic toxicants in wastewater

Contact Info

Product

Resources

About