scholarly journals Pd/Au Based Catalyst Immobilization in Polymeric Nanofibrous Membranes via Electrospinning for the Selective Oxidation of 5-Hydroxymethylfurfural

Processes ◽  
2020 ◽  
Vol 8 (1) ◽  
pp. 45 ◽  
Author(s):  
Danilo Bonincontro ◽  
Francesco Fraschetti ◽  
Claire Squarzoni ◽  
Laura Mazzocchetti ◽  
Emanuele Maccaferri ◽  
...  
Keyword(s):  
Selective Oxidation ◽  
Large Scale ◽  
Catalytic Performance ◽  
High Yield ◽  
Key Factors ◽  
Hydroxymethyl Furfural ◽  
Catalyst Immobilization ◽  
Polymeric Component ◽  
Furandicarboxylic Acid ◽  
Nanofibrous Membranes

Innovative nanofibrous membranes based on Pd/Au catalysts immobilized via electrospinning onto different polymers were engineered and tested in the selective oxidation of 5-(hydroxymethyl)furfural in an aqueous phase. The type of polymer and the method used to insert the active phases in the membrane were demonstrated to have a significant effect on catalytic performance. The hydrophilicity and the glass transition temperature of the polymeric component are key factors for producing active and selective materials. Nylon-based membranes loaded with unsupported metal nanoparticles were demonstrated to be more efficient than polyacrylonitrile-based membranes, displaying good stability and leading to high yield in 2,5-furandicarboxylic acid. These results underline the promising potential of large-scale applications of electrospinning for the preparation of catalytic nanofibrous membranes to be used in processes for the conversion of renewable molecules.

Adhesive Catalyst Immobilization of Palladium Nanoparticles on Cotton and Filter Paper: Applications to Reusable Catalysts for Sequential Catalytic Reactions

2014 ◽  
Vol 356 (5) ◽  
pp. 951-960 ◽  
Author(s):  
Takashi Nishikata ◽  
Hironori Tsutsumi ◽  
Lei Gao ◽  
Keisuke Kojima ◽  
Katsumi Chikama ◽  
...  
Keyword(s):  
Filter Paper ◽  
Palladium Nanoparticles ◽  
Catalytic Reactions ◽  
Catalyst Immobilization

Méthodes de qualification des immobilisations chimiques d'une enzyme sur un support solide

2005 ◽  
Vol 83 (1) ◽  
pp. 70-77 ◽  
Author(s):  
Anne Belzil ◽  
Carmen Parent
Keyword(s):  
Carbonic Anhydrase ◽  
Covalent Binding ◽  
Qualitative Evaluation ◽  
Solid Support ◽  
Catalytic Transformation ◽  
Enzyme Binding ◽  
Bicarbonate Ions ◽  
Catalyst Immobilization ◽  
Immobilization Enzyme

Carbonic anhydrase was immobilized on a polymer thermoplastic to promote gaseous CO2 hydration into bicarbonate ions. Catalyst immobilization was realized through a series of chemical reactions enabling enzyme covalent binding to polyamide support. Different initial enzyme concentrations of 0.25, 0.50, 0.75, 1, and 2 mg/ml were verified. Different techniques were developed to assess enzyme attachment. The amount of bound protein was determined using Bradford dosage of proteins remaining in solution following CA II incubation with solid support. ELISA has given a qualitative evaluation of the protein, enabling a follow up of enzyme binding robustness as a function of time. p-nitrophenyl acetate hydrolysis and CO2 hydration were assessed by spectrophotometry and electrometry, respectively. The percentage of active enzyme following immobilization was measured using an esterase linear model. Catalytic transformation rates for gaseous CO2 hydration were calculated for each type of immobilization.Key words: immobilization, enzyme, esterase, hydration.[Journal translation]

scholarly journals Silk Fibroin-Based Materials for Catalyst Immobilization

Molecules ◽  
2020 ◽  
Vol 25 (21) ◽  
pp. 4929
Author(s):  
Shanshan Lv
Keyword(s):  
Silk Fibroin ◽  
Phenylalanine Ammonia Lyase ◽  
Organophosphorus Hydrolase ◽  
Future Research ◽  
Research Directions ◽  
Catalyst Immobilization ◽  
Composition And Structure ◽  
Immobilization Of Enzymes ◽  
Future Research Directions ◽  
Unique Amino Acid

Silk fibroin is a widely and commercially available natural protein derived from silkworm cocoons. Thanks to its unique amino acid composition and structure, which lead to localized nanoscale pockets with limited but sufficient hydration for protein interaction and stabilization, silk fibroin has been studied in the field of enzyme immobilization. Results of these studies have demonstrated that silk fibroin offers an important platform for covalent and noncovalent immobilization of enzymes through serving as a stabilization matrix/support with high retention of the biological activity of the enzymes of interest. In the hope of providing suggestions for potential future research directions, this review has been written to briefly introduce and summarize key advances in silk fibroin-based materials for immobilization of both enzymes/biocatalysts (including alkaline phosphatase, β-glucosidase, glucose oxidase, lipase, urease, uricase, horseradish peroxidase, catalase, xanthine oxidase, tyrosinase, acetylcholinesterase, neutral protease, α-chymotrypsin, amylase, organophosphorus hydrolase, β-galactosidase, carbonic anhydrase, laccase, zymolyase, phenylalanine ammonia-lyase, thymidine kinase, and several others) and non-enzymatic catalysts (such as Au, Pd, Fe, α-Fe2O3, Fe3O4, TiO2, Pt, ZnO, CuO, Cu2O, Mn3O4, and MnO2).

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