Expression, Purification, Structural and Functional Characterization of Recombinant 11S Edestin in <i>Escherichia coli</i>, a typical seed storage globulin from <i>Cannabis sativa</i> L.

Hemp seed protein consists of about 80% globulin (11S edestin) and 20% albumin (2S albumin) and attracts worldwide attention because of its superior nutritional value, hypoallergenicity, high digestibility, and functional activities. However, the difficulties of obtaining a single protein component due to low spatiotemporal output, low purity, and residual issues of toxic reagents limit the characterization of each protein and its precision applications in food and biomedicine. In this study, hemp seed globulin was produced in <i>E. coli</i> cell factory (recombinant 11S edestin) for the first time to compare the structural differences, morphology, thermal stability, and emulsifying activity with the traditionally salt-extracted hemp seed globulin (SHSG). This study revealed notable differences between them, which can probably be attributed to their distinct structural and morphological features. This study lays a good foundation for further academic research and industrial development of recombinant hemp seed proteins including 11S edestin.