Strategies for Optimizing the Yield and Function of Recombinant Collagen in Different Expression Systems: A Review

Collagen is the most abundant structural and functional protein in humans and other vertebrates. It possesses remarkable biological functions and is widely used in food, cosmetics, and healthcare. Currently, mainstream animal-derived collagen materials carry risks such as viral transmission and allergic reactions. However, recombinant collagen, heterologously expressed using genetic recombination technology combined with high-density fermentation processes, offers greater biocompatibility, low immunogenicity, and consistent quality, offering promising development prospects. However, current research on recombinant collagen still faces challenges such as low yield and poor functionality. This article briefly describes the structure, types, and functions of collagen, discusses the advantages and limitations of different recombinant collagen expression systems, and highlights the strategies for improving the yield and optimizing the function of recombinant collagen, ranging from gene editing to fermentation optimization. In highlighting practical approaches to achieving high yield, we present a series of case examples to illustrate the successful application of these principles. This review aims to help researchers, engineers, and industry practitioners better understand research trends in the expression and production of recombinant collagen, and to promote its further development and commercialization across diverse application areas.

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Publication Details

Journal
International Journal of Molecular Sciences
Published
2026-03-11
DOI
https://doi.org/10.3390/ijms27062563
Primary Topic
Collagen: Extraction and Characterization
Type
article
Field-Weighted Citation Impact
0.00

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article

Strategies for Optimizing the Yield and Function of Recombinant Collagen in Different Expression Systems: A Review

Zhiqiang Xiong, Lan Jiang, Ziyi Zhang, Menglei Cheng et al.
International Journal of Molecular Sciences
Collagen: Extraction and Characterization
article

Strategies for Optimizing the Yield and Function of Recombinant Collagen in Different Expression Systems: A Review

Zhiqiang Xiong, Lan Jiang, Ziyi Zhang, Menglei Cheng, X. H. Liu, Lianzhong Ai, Guangqiang Wang, Liuzhu Ji
article en

Abstract

Collagen is the most abundant structural and functional protein in humans and other vertebrates. It possesses remarkable biological functions and is widely used in food, cosmetics, and healthcare. Currently, mainstream animal-derived collagen materials carry risks such as viral transmission and allergic reactions. However, recombinant collagen, heterologously expressed using genetic recombination technology combined with high-density fermentation processes, offers greater biocompatibility, low immunogenicity, and consistent quality, offering promising development prospects. However, current research on recombinant collagen still faces challenges such as low yield and poor functionality. This article briefly describes the structure, types, and functions of collagen, discusses the advantages and limitations of different recombinant collagen expression systems, and highlights the strategies for improving the yield and optimizing the function of recombinant collagen, ranging from gene editing to fermentation optimization. In highlighting practical approaches to achieving high yield, we present a series of case examples to illustrate the successful application of these principles. This review aims to help researchers, engineers, and industry practitioners better understand research trends in the expression and production of recombinant collagen, and to promote its further development and commercialization across diverse application areas.

International Journal of Molecular SciencesVol. 27(6)
University of Shanghai for Science and Technology (CN), Shanghai Jiao Tong University (CN)
Natural Science Foundation of Shanghai, National Natural Science Foundation of China
Openalex Percentile: Top 30%
Collagen: Extraction and Characterization
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