Polydopamine tethered enzyme/metal-organic framework composites with high stability and reusability.

Nanoscale

Key Lab for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing 100084, China.

Published: December 2015

An enzyme/metal-organic framework (MOF) composite with both highly stable and easily reusable features was prepared via tethering enzyme/MOF nanocrystals with polydopamine (PDA). The micrometer-sized PDA tethered enzyme/MOF composite can be easily repeatedly used without obvious activity loss, promising for efficient enzymatic catalysis at low cost with long-term operational stability under harsh conditions.

Download full-text PDF

Source
http://dx.doi.org/10.1039/c5nr05190hDOI Listing

Publication Analysis

Top Keywords

enzyme/metal-organic framework
8
polydopamine tethered
4
tethered enzyme/metal-organic
4
framework composites
4
composites high
4
high stability
4
stability reusability
4
reusability enzyme/metal-organic
4
framework mof
4
mof composite
4

Similar Publications

Pathogenic bacteria have consistently posed a formidable challenge to human health, creating the critical need for effective antibacterial solutions. In response, enzyme-metal-organic framework (MOF) composites have emerged as a promising class of antibacterial agents. This study focuses on the development of an enzyme-MOF composite based on HZIF-8, incorporating the advantages of simple synthesis, ZIF-8 antibacterial properties, lysozyme hydrolysis, and high biological safety.

View Article and Find Full Text PDF

Enzyme-incorporated composites with hierarchical porous structures can lead to improved performance of hybrid biocatalysts. Metal-organic frameworks (MOFs) have recently emerged as excellent biomineralizable materials for forming hybrid biocatalysts, offering superior performance for biocatalytic reactions. However, the small nanopores of MOFs significantly reduce the diffusion rates of small substrate molecules, hindering the contact between the inner active sites of an enzyme and the molecules, lowering the biocatalytic efficiency.

View Article and Find Full Text PDF

Green synthesis of enzyme/metal-organic framework composites with high stability in protein denaturing solvents.

Bioresour Bioprocess

May 2017

Key Lab for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing, 100084 China.

Objectives: Enzyme/metal-organic framework composites with high stability in protein denaturing solvents were reported in this study.

Results: Encapsulation of enzyme in metal-organic frameworks (MOFs) via co-precipitation process was realized, and the generality of the synthesis was validated by using cytochrome c, horseradish peroxidase, and lipase B as model enzymes. The stability of encapsulated enzyme was greatly increased after immobilization on MOFs.

View Article and Find Full Text PDF

Polydopamine tethered enzyme/metal-organic framework composites with high stability and reusability.

Nanoscale

December 2015

Key Lab for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing 100084, China.

An enzyme/metal-organic framework (MOF) composite with both highly stable and easily reusable features was prepared via tethering enzyme/MOF nanocrystals with polydopamine (PDA). The micrometer-sized PDA tethered enzyme/MOF composite can be easily repeatedly used without obvious activity loss, promising for efficient enzymatic catalysis at low cost with long-term operational stability under harsh conditions.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!