Thermal denaturation and aggregation of hemoglobin of Glossoscolex paulistus in acid and neutral media

► DSC data show that HbGp unfolding is partially reversible at pH 7.0. ► AUC data show HbGp remains undissociated at 50 °C, fully dissociating above 60 °C. ► HbGp unfolding in neutral pH 7.0 is accompanied by aggregation, monitored by DLS. ► Protein concentration and temperature are critical in aggregation rate determination. ► HbGp is more stable in acidic medium than neutral solution, as it is shown by DSC and spectroscopy.