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Enzyme activity assay for horseradish peroxidase encapsulated in peptide nanotubes
- Source :
- Enzyme and Microbial Technology. 51:81-85
- Publication Year :
- 2012
- Publisher :
- Elsevier BV, 2012.
-
Abstract
- Encapsulation of horseradish peroxidase (HRP) inside a peptide nanotube (PNT) was demonstrated and its activity was measured. Enzyme assay verified that 0.16 μg of the enzymes were encapsulated in 1mg of PNTs. The encapsulation was also verified with TEM, UV-vis spectroscopy, and FTIR. The activity of the encapsulated HRP was examined for thermal stability, long-term storage stability, and resistance to a denaturant. They showed good storage stability, retaining its activity up to 90%, while the free HRP lost 50% of its activity over the course of 18 days. At 55 °C, the encapsulated HRP activity remained 20% higher than that of the free HRP. With the denaturant, guanidinium hydrochloride (GdmHCl), the encapsulated HRP activity was maintained around 10% higher than the free HRP. This result proves that the encapsulation of HRP inside the PNT may be an effective way to keep the enzyme activity stable in various environments.
- Subjects :
- Microscopy, Electron, Scanning Transmission
Nanotubes, Peptide
Protein Denaturation
Hydrochloride
Drug Compounding
Kinetics
Bioengineering
Peptide
Microscopy, Atomic Force
Applied Microbiology and Biotechnology
Biochemistry
Horseradish peroxidase
chemistry.chemical_compound
Enzyme Stability
Spectroscopy, Fourier Transform Infrared
Thermal stability
Guanidine
Horseradish Peroxidase
Enzyme Assays
chemistry.chemical_classification
Chromatography
biology
Chemistry
food and beverages
Enzymes, Immobilized
Enzyme assay
Enzyme
Microscopy, Electron, Scanning
biology.protein
Biotechnology
Subjects
Details
- ISSN :
- 01410229
- Volume :
- 51
- Database :
- OpenAIRE
- Journal :
- Enzyme and Microbial Technology
- Accession number :
- edsair.doi.dedup.....358fdb4127c28f986be3d7af017faf50