Soybean peroxidase immobilized on δ-FeOOH as new magnetically recyclable biocatalyst for removal of ferulic acid
Language English Country Germany Media print-electronic
Document type Journal Article
PubMed
28986654
DOI
10.1007/s00449-017-1848-1
PII: 10.1007/s00449-017-1848-1
Knihovny.cz E-resources
- Keywords
- Biocatalyst, Bioremediation, Iron oxide, Wastewater,
- MeSH
- Water Purification MeSH
- Enzymes, Immobilized chemistry MeSH
- Glycine max enzymology MeSH
- Catalysis MeSH
- Coumaric Acids chemistry MeSH
- Wastewater chemistry MeSH
- Silicon Dioxide chemistry MeSH
- Peroxidase chemistry MeSH
- Plant Proteins chemistry MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Enzymes, Immobilized MeSH
- ferulic acid MeSH Browser
- Coumaric Acids MeSH
- Waste Water MeSH
- Silicon Dioxide MeSH
- Peroxidase MeSH
- Plant Proteins MeSH
A significant enhancement in the catalytic performance due to enzymes immobilization is a great way to enhance the economics of biocatalytic processes. The soybean peroxidase (SP) immobilization under ferroxyte and the ferulic acid removal by the enzyme free and immobilized were investigated. The immobilization via silica-coated ferroxyte nanoparticles was effective, and immobilization yield of 39%. The scanning electron microscopy (SEM) images showed significant changes in the materials morphology. Substantial differences were observed in the particles' Fourier Transform Infrared (FTIR) spectra. The magnetic catalyst revealed a better performance than the free enzyme in the ferulic acid conversion, presenting a good V max/K m ratio when compared with the free enzyme. The reuse evaluated by ten cycles exhibited excellent recycling, remaining constant between the sixth and seventh cycles. The use of magnetic nanocatalyst becomes possible to eliminate the high operational costs, and complicated steps of the conventional enzymatic processes. Thus, a viable industrial route for the use of the enzyme as catalyst is possible.
Department of Chemistry Engineering Federal University of São Carlos 13565 905 São Carlos SP Brazil
Department of Chemistry Federal University of Lavras N° 37 37200 000 Lavras MG Brazil
Department of Chemistry Federal University of Minas Gerais 31270 901 Belo Horizonte MG Brazil
Department of Chemistry Federal University of Ouro Preto 35400 000 Ouro Preto MG Brazil
References provided by Crossref.org
Δ-FeOOH as Support for Immobilization Peroxidase: Optimization via a Chemometric Approach