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Preparation of multi-enzyme co-immobilized nanoparticles by bis-aryl hydrazone bond conjugation.
- Source :
-
Biotechnology and applied biochemistry [Biotechnol Appl Biochem] 2016 Mar-Apr; Vol. 63 (2), pp. 214-9. Date of Electronic Publication: 2015 May 29. - Publication Year :
- 2016
-
Abstract
- A novel multi-enzyme co-immobilized nanoparticle was prepared by the bis-aryl hydrazone conjugation strategy for enhancing the overall reaction efficiency and specificity. It can be seen that the molar substitution ratios of succinimidyl 6-hydrazinonicotinamid acetone hydrazone or succinimidyl 4-formylbenzoate to glucose oxidase (GOX) or horseradish peroxidase (HRP) increased with the concentration of the linking reagents. The amount of the immobilized conjugates on the support was measured to be 22.8 ± 1.6 mg/g-particle, and it meant that more than 90% of the GOX-HRP conjugates were successfully attached onto the polystyrene (PS) nanoparticles. Moreover, the immobilized bi-enzymes conjugate on the PS nanoparticles increased about 1.6-fold compared with that of free enzymes.<br /> (© 2015 International Union of Biochemistry and Molecular Biology, Inc.)
- Subjects :
- Enzymes, Immobilized metabolism
Glucose Oxidase metabolism
Horseradish Peroxidase metabolism
Hydrazones metabolism
Molecular Structure
Nanoparticles metabolism
Particle Size
Polystyrenes metabolism
Surface Properties
Enzymes, Immobilized chemistry
Glucose Oxidase chemistry
Horseradish Peroxidase chemistry
Hydrazones chemistry
Nanoparticles chemistry
Polystyrenes chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1470-8744
- Volume :
- 63
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biotechnology and applied biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 25676477
- Full Text :
- https://doi.org/10.1002/bab.1364