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
Hauptverfasser: Dong, Minmin, Zhang, Liyan, Li, Rui, Li, Shuying, Jiang, Yao, Qiao, Yuchun, Duan, Zhiqiang, Li, Ru, Wang, Quanfu, Wang, Hua
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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.
ISSN:2046-2069
2046-2069
DOI:10.1039/c6ra07139b