Enzyme properties and thermal stability of horseradish peroxidase (HRP-DL)
Te Wang, Jing Tian, Tingting Li, Jian Li
Available Online March 2016.
- https://doi.org/10.2991/iceti-16.2016.40How to use a DOI?
- Horseradish peroxidase, thermal stability, protective agent, stress resistance, Ectione
- Horseradish peroxidase (HRP) is widely used in biological engineering, wastewater treatment, enzyme-linked immunosorbent assay and other fields. It is great significance to study its enzyme properties, stress resistance and protective agent. In order to provide good quality HRP, and protection method of HRP thermal stability, horseradish peroxidase (HRP-DL) was extracted and purified from horseradish which was collected from Dalian, China in this paper. It was investigated that the enzyme characterization, thermal stability, thermal protection from thermal stability protection agents of HRP-DL. The optimum temperature of HRP-DL was 30 °C, the optimum pH of HRP-DL was 5.5. HRP-DL enzyme activity was inhibited significantly by NaCl. HRP-DL was activated by Ca2+, Mn2+, Zn2+, Pb2+, Mg2+, Go2+, Fe3+, and inhibited by K+, Cu2+, Hg2+, Ag+ and Fe2+ in different degree. When HRP-DL was processed at the temperature greater than or equal to 35 °C, the residual enzyme activity was reduced. The HRP-DL residual enzyme activity increase 49.3% when added 1 mmol/L Ectoine and heat treatment at 60 °C for 15 min. The study of HRP-DL enzyme characterization provided the basis for its practical application. Ectoine as HRP-DL thermally stable protective agent has advantages such as the use of less, the effect is significant.
- Open Access
- This is an open access article distributed under the CC BY-NC license.
Cite this article
TY - CONF AU - Te Wang AU - Jing Tian AU - Tingting Li AU - Jian Li PY - 2016/03 DA - 2016/03 TI - Enzyme properties and thermal stability of horseradish peroxidase (HRP-DL) BT - 2016 International Conference on Engineering and Technology Innovations PB - Atlantis Press SN - 2352-5401 UR - https://doi.org/10.2991/iceti-16.2016.40 DO - https://doi.org/10.2991/iceti-16.2016.40 ID - Wang2016/03 ER -