Enzyme properties and thermal stability of horseradish peroxidase (HRP-DL)

Abstract

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 Ca 2+ , Mn 2+ , Zn 2+ , Pb 2+ , Mg 2+ , Go 2+ , Fe 3+ , and inhibited by K + , Cu 2+ , Hg 2+ , Ag + , Fe 2+ 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.

Peroxidase inhibitory and antioxidant constituents from Juniperus L. species guided by HPTLC-bioautography and molecular docking studies

“…Peak area was plotted against plant extract concentration in µg/spot to construct the calibration curve, followed by subjection of the calibration data to least-squares regression analysis. Thereafter, peroxidase inhibition activity of the samples was detected by immersion of plates in the enzyme solution for 3s followed by activation of the enzyme by putting the plate in an oven at 35 ο C (Wang et al 2016) for 2 min and finally dipping the plate in H 2 O 2 and Benzidine solution, separately and respectively.…”

Multibranched Au–Ag–Pt Nanoparticle as a Nanozyme for the Colorimetric Assay of Hydrogen Peroxide and Glucose

“…Natural enzymes are mainly protein-based compounds, and enzyme activity is greatly affected by the changes in temperature, pH, and salt concentration. 3 In a study that confirmed the enzymatic activity of peroxidase, the enzyme activity decreased by 30% when the temperature was near the body temperature. Outside a pH of 7, the enzyme activity sharply dropped, and the enzyme activity sharply dropped even with a change in the salt concentration.…”

“…However, the peroxidase used in this process is a natural enzyme derived from living organisms. Natural enzymes are mainly protein-based compounds, and enzyme activity is greatly affected by the changes in temperature, pH, and salt concentration . In a study that confirmed the enzymatic activity of peroxidase, the enzyme activity decreased by 30% when the temperature was near the body temperature.…”