Thermal treatment modified the physicochemical properties of recombinant oyster (Crassostrea gigas) ferritin.

The unique nanocage structure of ferritin can be used as functional nanomaterials and has wide application prospects. However, thermal treatment may affect the structure of ferritin, further affecting self-assembly property. In this study, the oyster ferritin gene GF1 was obtained, prokaryotically expressed in E. coli BL21 (DE3). Then the purified ferritin was heated from 60 to 100 °C for 10 min with untreated ferritin as a control sample. The aggregation state of ferritin was investigated and the difference in protein structure was evaluated in terms of particle size and protein structures. The results of electrophoresis indicated that thermal treatment induced denaturation and aggregation of ferritin macromolecules. Moreover, the particle size distribution shifted to larger size trend and aggregates were visible with the heated samples and the secondary structure and tertiary structure were destroyed gradually. The findings are beneficial for understanding the relationship of the structure and function of ferritin.