Scale up of fermentation of recombinant Escherichia coli for efficient production of spider drag silk protein MaSp1s and its dimers

This study successfully addressed key challenges in recombinant spidroin production by employing fusion tags (SUMO and self-shearing peptide intein) to enable the soluble expression of rMaSp1 and its dimer rMaSp1s-2Core. The secondary structure and self-assembly analyses further contributed to our understanding of recombinant spidroin. These findings enable the large-scale production of spidroin and its potential applications in the biomedical, chemical, and military industries, overcoming previous hurdles related to the solubility and toxicity associated with downstream processing.