immobilization of genetically-modified d-amino acid oxidase and catalase on carbon nanotubes to improve the catalytic efficiency
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ID: 246299
2016
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Abstract
d-amino acid oxidase (DAAO) and catalase (CAT) have been genetically modified by fusing them to an elastin-like polypeptide (ELP). ELP-DAAO and ELP-CAT have been separately immobilized on multi-walled carbon nanotubes (MWNTs). It has been found that the secondary structures of the enzymes have been preserved. ELP-DAAO catalyzed the oxidative deamination of d-alanine, and H2O2 was evolved continuously. When the MWNT-supported enzymes were used together, the generated hydrogen peroxide of ELP-DAAO could be decomposed in situ. The catalytic efficiency of the two immobilized enzymes was more than five times greater than that of free ELP-DAAO when the ratio of immobilized ELP-CAT to immobilized ELP-DAAO was larger than 1:1.
| Reference Key |
li2016catalystsimmobilization
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|---|---|
| Authors | ;Rong Li;Jian Sun;Yaqi Fu;Kun Du;Mengsha Cai;Peijun Ji;Wei Feng |
| Journal | journal of essential oil research |
| Year | 2016 |
| DOI |
10.3390/catal6050066
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