A comprehensive overview of recombinant type III collagen (rhCOL III) spanning molecular design to practical applications (The structure of the recombinant collagen molecule is derived from PDB ID 6A0A 1 ). • This review provides a comprehensive examination of Type III collagen, with particular emphasis on its unique triple helix structure, which confers distinctive biological properties and functional characteristics. • The review further explores its essential roles in various physiological and pathological processes, such as wound healing, skin aging, and cardiovascular diseases, while also addressing current challenges and future research directions in the field. Collagen, the most abundant protein in mammals, constitutes approximately 30 % of the total protein content in the human body and plays a critical role in maintaining tissue structure and function. Among various types, type III collagen is a key component of the extracellular matrix and features a distinctive triple-helical structure that confers specific biological activities and functional properties. However, its production has long been constrained by low expression levels and an unstable triple helix structure. With advances in genetic engineering and synthetic biology, significant progress has been achieved in the research and application of recombinant type III collagen (rhCOL III). This review focuses on recent developments in expression systems, particularly in Escherichia coli and Pichia pastoris , where production yields have reached 3.02 g/L and 10.3 g/L respectively. Recombinant type III collagen has found applications in diverse fields, including skincare, injectable fillers, wound dressings, and tissue engineering. Future development directions include AI-driven molecular design, 3D bioprinting, and large-scale fermentation processes, aimed at addressing current challenges related to proline hydroxylation, purification efficiency, and immunogenicity.
Wang et al. (2026) studied this question.