Journal
CATALYSTS
Volume 6, Issue 5, Pages -Publisher
MDPI
DOI: 10.3390/catal6050066
Keywords
D-amino acids oxidase; catalase; elastin-like polypeptide; immobilization; carbon nanotubes
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Funding
- National Science Foundation of China [21376021, 21576018]
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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.
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