Crosslinking catalysis-active center of hemin on the protein scaffold toward peroxidase mimic with powerful catalysis
An enzyme mimic synthesis protocol has been proposed by simply cross-linking the redox active center of peroxidase onto a protein scaffold. Colorimetric assays and kinetic studies indicate that the developed peroxidase mimic can present much stronger catalysis and better aqueous stability than nativ...
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Veröffentlicht in: | RSC advances 2016-01, Vol.6 (53), p.47595-47599 |
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Hauptverfasser: | , , , , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | An enzyme mimic synthesis protocol has been proposed by simply cross-linking the redox active center of peroxidase onto a protein scaffold. Colorimetric assays and kinetic studies indicate that the developed peroxidase mimic can present much stronger catalysis and better aqueous stability than native hemin.
Catalytic hemin (Hem) was cross-linked onto the protein scaffold of bovine serum albumin (BSA) forming a Hem-BSA composite with powerful catalysis. |
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ISSN: | 2046-2069 2046-2069 |
DOI: | 10.1039/c6ra07139b |