reaction activity in the presence of recombinant BPO-A1 peaks at 60°C whereas peak in the non-enzymatic activity of H2O2 is not observed in temperature range of 10-70°C. The increase in the activity of the enzyme with propanoic acid around 10-50°C is due to the peroxidation step because high activity in the nonenzymatic oxidative bromination step is maintained at low temperature, which suppresses the decomposition of the active species generated by the reaction between peracid and Br-. The active species is heat-labile. The significant decrease in activity around 65-70°C is attributed to decomposition of the active species. The native BPO-A1 possesses high stability up to 80°C. Recombinant BPO-A1 possesses high peroxidating activity at high temperatures
the oligomeric structure of the enzyme is not apparently disrupted by exposure to 60°C. The purified bromoperoxidase at 135 nM is maintained in the absence of any protective reagent at 60°C for 24 h. Within 30 min about 60% of the original activity is lost but no further decline in activity is seen over the full course of the incubation
vanadate increases the thermostability. Ag+ and Al3+ lower the thermostability of the enzyme when compared with the control. Mn2+, Fe2+, Co2+, Ni2+, and Ba2+ have slightly positive effects, whereas Li+, Na+, K+, and Rb+ have no effect and Zn2+ lowers the thermostability