Immobilization of Lipase Onto Dopamine Functionalized Magnetic Nanoparticles

Zhuang, Meng-Yao; Zhou, Qian-Liu; Wang, Xiangyu; Xue, Lan; Wang, Ru; Zhang, Jiu-Xun; Zhang, Ye-Wang

doi:10.1166/nnl.2016.2127

Cited by 13 publications

(6 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Immobilization of an enzyme involves the interactions between the enzyme and the carrier [8][9][10][11][12]. The properties of the carrier play an important role and normally the carrier should have large surface area [13][14][15].…”

Section: Introductionmentioning

confidence: 99%

Rapid Immobilization of Cellulase onto Graphene Oxide with a Hydrophobic Spacer

Gao

Wang

et al. 2018

Catalysts

Self Cite

View full text Add to dashboard Cite

A rapid immobilization method for cellulase was developed. Functional graphene oxide was synthesized and grafted with hydrophobic spacer P-β-sulfuric acid ester ethyl sulfone aniline (SESA) though etherification and diazotization. The functionalized graphene oxide was characterized by Fourier-transform infrared spectroscopy and was used as the carrier for the immobilization of cellulase via covalent binding. The immobilization of cellulase was finished in a very short time (10 min) and very high immobilization yield and efficiency of above 90% were achieved after optimization. When compared with the free cellulase, thermal and operational stabilities of the immobilized cellulase were improved significantly. At 50 °C, the half-life of the immobilized cellulase (533 min) was six-fold higher than that of the free cellulase (89 min). Additionally, the affinity between immobilized cellulase (Km = 2.19 g L −1 ) and substrate was more favorable than that of free cellulase (Km = 3.84 g L −1 ), suggesting the immobilized cellulase has higher catalytic efficiency. The possible immobilization mechanism was proposed. The results strongly indicate that the immobilization is highly efficient and has great potential for the immobilization of other enzymes.

show abstract

Section: Introductionmentioning

confidence: 99%

Rapid Immobilization of Cellulase onto Graphene Oxide with a Hydrophobic Spacer

Gao

Wang

et al. 2018

Catalysts

Self Cite

View full text Add to dashboard Cite

show abstract

“…These results demonstrated that the mannose was successfully functionalized onto the magnetic Fe 3 O 4 @OA@DP nanoparticles. The preparation of nanoparticles, including Fe3O4, Fe3O4@OA (oleic acid), and Fe3O4@OA@DP (dopamine), and the characterization of these nanoparticles using Fourier transform infrared spectroscopy (FTIR) and transmission electron microscopy (TEM) have been reported in our previous work [35]. To demonstrate that mannose was successfully anchored onto the surface of magnetic Fe3O4@OA@DP, the nanoparticles were analyzed using FTIR.…”

Section: Characterization Of the Nanoparticlesmentioning

confidence: 99%

Specific Immobilization of Escherichia coli Expressing Recombinant Glycerol Dehydrogenase on Mannose-Functionalized Magnetic Nanoparticles

Zhuang

Shen

et al. 2018

Catalysts

Self Cite

View full text Add to dashboard Cite

Mannose-functionalized magnetic nanoparticles were prepared for the immobilization of Escherichia coli cells harboring the recombinant glycerol dehydrogenase gene. Immobilization of whole E. coli cells on the carrier was carried out through specific binding between mannose on the nanoparticles and the FimH lectin on the E. coli cell surface via hydrogen bonds and hydrophobic interactions. The effects of various factors including cell concentration, pH, temperature, and buffer concentration were investigated. High degrees of immobilization (84%) and recovery of activity (82%) were obtained under the following conditions: cell/support 1.3 mg/mL, immobilization time 2 h, pH 8.0, temperature 4°C, and buffer concentration 50 mM. Compared with the free cells, the thermostability of the immobilized cells was improved 2.56-fold at 37 °C. More than 50% of the initial activity of the immobilized cells remained after 10 cycles. The immobilized cells were evaluated functionally by monitoring the catalytic conversion of glycerol to 1,3-dihydroxyacetone (DHA). After a 12 h reaction, the DHA produced by the immobilized cells was two-fold higher than that produced by the free cells. These results indicate that mannose-functionalized magnetic nanoparticles can be used for the specific recognition of gram-negative bacteria, which gives them great potential in applications such as the preparation of biocatalysts and biosensors and clinical diagnosis.

show abstract

“…Numerous covalent bond-based methods have been directly used in nanomaterials recently [44,45]. These nanomaterials can be tailored to the target enzyme, and their large surface area and selectivity of porosity provide great advantages in industrial and pharmaceutical products [6,[46][47][48].…”

Section: Covalent Bondingmentioning

confidence: 99%

Recent Developments in Carriers and Non-Aqueous Solvents for Enzyme Immobilization

2019

View full text Add to dashboard Cite

Immobilization techniques are generally based on reusing enzymes in industrial applications to reduce costs and improve enzyme properties. These techniques have been developing for decades, and many methods for immobilizing enzymes have been designed. To find a better immobilization method, it is necessary to review the recently developed methods and have a clear overview of the advantages and limitations of each method. This review introduces the recently reported immobilization methods and discusses the improvements in enzyme properties by different methods. Among the techniques to improve enzyme properties, metal–organic frameworks, which have diverse structures, abundant organic ligands and metal nodes, offer a promising platform.

show abstract

Immobilization of Lipase Onto Dopamine Functionalized Magnetic Nanoparticles

Cited by 13 publications

References 0 publications

Rapid Immobilization of Cellulase onto Graphene Oxide with a Hydrophobic Spacer

Rapid Immobilization of Cellulase onto Graphene Oxide with a Hydrophobic Spacer

Specific Immobilization of Escherichia coli Expressing Recombinant Glycerol Dehydrogenase on Mannose-Functionalized Magnetic Nanoparticles

Recent Developments in Carriers and Non-Aqueous Solvents for Enzyme Immobilization

Contact Info

Product

Resources

About