Expression, optimization and biological activity analysis of recombinant type III collagen in Komagataella phaffii.

Type III collagen, a fundamental constituent of the extracellular matrix (ECM), is extensively utilized across the biomedicine, tissue engineering, and cosmetic industries because of its exceptional biocompatibility and biodegradability. Despite its widespread application, traditional methods of collagen production are often hindered by the limit yield, potential immunogenicity, and batch-to-batch variability. In the present study, we describe a synthetic biological approach for expressing full-length recombinant type III collagen (RCIII) in the Komagataella phaffii system. Furthermore, the protein expression level was effectively increased by co-expression of the MPR1 gene, which improved the intrinsic antioxidant defenses of yeast cells, thereby reducing oxidative stress damage. The resulting RCIII maintains its native secondary structure and exhibits robust biological activities, including the promotion of platelet coagulation, enhancement of cell migration, and anti-inflammatory efficacy. Our findings suggest a viable pathway for large-scale, industrial production of type III collagen, offering a promising biomaterial for advanced biomedical applications, and contributing to the circular economy of the biomedical sector.