{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,31]],"date-time":"2026-08-31T15:54:29Z","timestamp":1788191669187,"version":"build-2803163510"},"reference-count":66,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2026,3,11]],"date-time":"2026-03-11T00:00:00Z","timestamp":1773187200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Key Project of Synthetic Biology of Shanghai \u201cScience and Technology Innovation Action Plan\u201d","award":["23HC1400900"],"award-info":[{"award-number":["23HC1400900"]}]},{"DOI":"10.13039\/100007219","name":"Shanghai Natural Science Foundation","doi-asserted-by":"publisher","award":["25ZR1402389"],"award-info":[{"award-number":["25ZR1402389"]}],"id":[{"id":"10.13039\/100007219","id-type":"DOI","asserted-by":"publisher"}]},{"name":"\u201cSynthetic Biology\u201d Project of the Shanghai Key Technology R&D Program","award":["25HC2830500"],"award-info":[{"award-number":["25HC2830500"]}]},{"DOI":"10.13039\/501100001809","name":"Natural Science Foundation of China","doi-asserted-by":"crossref","award":["32025029"],"award-info":[{"award-number":["32025029"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Shanghai Engineering Research Center of food microbiology program","award":["19DZ2281100"],"award-info":[{"award-number":["19DZ2281100"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.3390\/ijms27062563","type":"journal-article","created":{"date-parts":[[2026,3,11]],"date-time":"2026-03-11T09:00:37Z","timestamp":1773219637000},"page":"2563","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Strategies for Optimizing the Yield and Function of Recombinant Collagen in Different Expression Systems: A Review"],"prefix":"10.3390","volume":"27","author":[{"given":"Menglei","family":"Cheng","sequence":"first","affiliation":[{"name":"Shanghai Engineering Research Center of Food Microbiology, School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lisheng","family":"Jiang","sequence":"additional","affiliation":[{"name":"Shanghai Engineering Research Center of Food Microbiology, School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zejia","family":"Zhang","sequence":"additional","affiliation":[{"name":"Shanghai Engineering Research Center of Food Microbiology, School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Liuzhu","family":"Ji","sequence":"additional","affiliation":[{"name":"Shanghai Engineering Research Center of Food Microbiology, School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhiqiang","family":"Xiong","sequence":"additional","affiliation":[{"name":"Shanghai Engineering Research Center of Food Microbiology, School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3966-044X","authenticated-orcid":false,"given":"Guangqiang","family":"Wang","sequence":"additional","affiliation":[{"name":"Shanghai Engineering Research Center of Food Microbiology, School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lianzhong","family":"Ai","sequence":"additional","affiliation":[{"name":"Shanghai Engineering Research Center of Food Microbiology, School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China"},{"name":"Department of Food Science & Technology, School of Agriculture and Biology, Shanghai Jiao Tong University, 800 Dongchuan Road, Shanghai 200240, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5988-7473","authenticated-orcid":false,"given":"Xinxin","family":"Liu","sequence":"additional","affiliation":[{"name":"Shanghai Engineering Research Center of Food Microbiology, School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,3,11]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1955","DOI":"10.1242\/jcs.03453","article-title":"Collagens at a glance","volume":"120","author":"Kadler","year":"2007","journal-title":"J. Cell Sci."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.1016\/j.msec.2019.02.070","article-title":"Recent advances of collagen-based biomaterials: Multi-hierarchical structure, modification and biomedical applications","volume":"99","author":"Liu","year":"2019","journal-title":"Mater. Sci. Eng. C"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1038\/nmat4089","article-title":"Bioinspired structural materials","volume":"14","author":"Wegst","year":"2015","journal-title":"Nat. Mater."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"49","DOI":"10.4161\/bioe.26002","article-title":"Human collagen produced in plants: More than just another molecule","volume":"5","author":"Shoseyov","year":"2014","journal-title":"Bioengineered"},{"key":"ref_5","first-page":"3228","article-title":"Industrial development history of recombinant collagen and prospects for its biomedical applications","volume":"38","author":"Fu","year":"2022","journal-title":"Chin. J. Biotechnol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1049\/enb.2017.0003","article-title":"Production of recombinant collagen: State of the art and challenges","volume":"1","author":"Wang","year":"2017","journal-title":"Eng. Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1006\/bbrc.1997.6069","article-title":"Formation of recombinant triple-helical [\u03b11 (IV)] 2\u03b12 (IV) collagen molecules in CHO cells","volume":"231","author":"Fukuda","year":"1997","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_8","first-page":"12","article-title":"Recombinant protein scaffolds for tissue engineering","volume":"7","author":"Ramshaw","year":"2012","journal-title":"Biomed. Mater."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1146\/annurev.biochem.77.032207.120833","article-title":"Collagen structure and stability","volume":"78","author":"Shoulders","year":"2009","journal-title":"Annu. Rev. Biochem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1002\/1097-0282(2000)55:6<436::AID-BIP1019>3.0.CO;2-D","article-title":"Collagen model peptides: Sequence dependence of triple-helix stability","volume":"55","author":"Persikov","year":"2000","journal-title":"Biopolymers"},{"key":"ref_11","first-page":"a004978","article-title":"The collagen family. Cold Spring Harb","volume":"3","year":"2011","journal-title":"Perspect. Biol."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Richards, A.J., and Snead, M.P. (2022). Molecular basis of pathogenic variants in the fibrillar collagens. Genes, 13.","DOI":"10.3390\/genes13071199"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Fertala, A. (2020). Three decades of research on recombinant colla gens: Reinventing the wheel or developing new biomedical products?. Bioengineering, 7.","DOI":"10.3390\/bioengineering7040155"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1002\/humu.20736","article-title":"Cells expressing partially unfolded R789C\/p.R989C type II procollagen mutant associated with spondyloepiphyseal dysplasia undergo apopto sis","volume":"29","author":"Hintze","year":"2008","journal-title":"Hum. Mutat."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1038\/nrm954","article-title":"Formation and transfer of disul phide bonds in living cells","volume":"3","author":"Sevier","year":"2002","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1111\/j.1432-1033.1980.tb04610.x","article-title":"Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. role of disulfide bridges and peptide bond isomer ization","volume":"106","author":"Bruckner","year":"1980","journal-title":"Eur. J. Biochem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/0022-2836(91)90885-A","article-title":"Analysis of structural design features in collagen","volume":"218","author":"Jones","year":"1991","journal-title":"J. Mol. Biol."},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Brinckmann, J., Notbohm, H., and M\u00fcller, P.K. (2005). Collagen: Primer in Structure, Processing, and Assembly, Springer.","DOI":"10.1007\/b98359"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"905","DOI":"10.3390\/biology11060905","article-title":"Collagen extraction from animal skin","volume":"11","author":"Matinong","year":"2022","journal-title":"Biology"},{"key":"ref_20","first-page":"105","article-title":"Enzymatic extraction and characterisation of a thermostable collagen from swim bladder of rohu (Labeo rohita)","volume":"97","author":"Nidheesh","year":"2016","journal-title":"J. Sci. Food Agric."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"665","DOI":"10.5851\/kosfa.2016.36.5.665","article-title":"Isolation and characterization of pepsin-soluble collagens from bones, skins, and tendons in duck feet","volume":"36","author":"Kim","year":"2016","journal-title":"Korean J. Food Sci. Anim. Resour."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/s11274-025-04276-z","article-title":"Innovations and challenges in collagen and gelatin production through precision fermentation","volume":"41","author":"Karp","year":"2025","journal-title":"World J. Microbiol. Biotechnol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/S0934-8832(11)80045-4","article-title":"Expression of human COL1A1 gene in stably transfected HT1080 cells: The production of a thermostable homotrimer of type I collagen in a recombinant system","volume":"13","author":"Geddis","year":"1993","journal-title":"Matrix"},{"key":"ref_24","unstructured":"National Medical Products Administration (NMPA) (2023). Guideline on Evaluation of Recombinant Humanized Collagen Raw Materials, Center for Medical Device Evaluation, NMPA. No. 16 of 2023."},{"key":"ref_25","unstructured":"(2022). Recombinant Collagen (Standard No. YY\/T 1849-2022)."},{"key":"ref_26","first-page":"71","article-title":"Recent advances in optimization strategies and applications of plant bioreactors","volume":"43","author":"Zou","year":"2023","journal-title":"China Biotechnol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2189","DOI":"10.1007\/s00438-016-1251-7","article-title":"Production of human type II collagen using an efficient baculovirus-silkworm multigene expression system","volume":"291","author":"Qi","year":"2016","journal-title":"Mol. Genet. Genom."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.3109\/07388551.2015.1084264","article-title":"Advanced technologies for improved expression of recombinant proteins in bacteria: Perspectives and applications","volume":"36","author":"Gupta","year":"2016","journal-title":"Crit. Rev. Biotechnol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.cobme.2019.06.001","article-title":"Recent progress with recombinant collagens produced in Escherichia coli","volume":"10","author":"Ramshaw","year":"2019","journal-title":"Curr. Opin. Biomed. Eng."},{"key":"ref_30","unstructured":"Chang, H.Y. (2009). Study on the Process of Recombinant E. coli High-Density Fermentation for Expressing Human-like Collagen II. [Doctoral Dissertation, Northwest University]."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"106473","DOI":"10.1016\/j.pep.2024.106473","article-title":"Preparation and characterization of a novel humanized collagen III with repeated fragments of Gly300-Asp329","volume":"219","author":"Yan","year":"2024","journal-title":"Protein Expr. Purif."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1007\/s10930-017-9723-0","article-title":"Hydroxylation of human type III collagen alpha chain by recombinant coexpression with a viral prolyl 4-hydroxylase in E. coli","volume":"36","author":"Shi","year":"2017","journal-title":"Protein J."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1046\/j.0022-202x.2001.01431.x","article-title":"Subcutaneous adipocytes promote the differentiation of squamous cell carcinoma cell line (DJM-1) in collagen gel matrix culture","volume":"117","author":"Inoue","year":"2001","journal-title":"J. Investig. Dermatol."},{"key":"ref_34","first-page":"354","article-title":"Pichia pastoris: A workhorse for recombinant protein production","volume":"2","author":"Fickers","year":"2014","journal-title":"Curr. Res. Microbiol. Biotechnol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1111\/j.1574-6976.2000.tb00532.x","article-title":"Heterologous protein expression in the methylotrophic yeast Pichia pastoris","volume":"24","author":"Cereghino","year":"2000","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/j.gene.2013.01.062","article-title":"The effect of \u03b1-mating factor secretion signal mutations on recombinant protein expression in Pichia pastoris","volume":"519","author":"Stark","year":"2013","journal-title":"Gene"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1093\/protein\/14.6.447","article-title":"Secreted production of a custom-designed, highly hydrophilic gelatin in Pichia pastoris","volume":"14","author":"Werten","year":"2001","journal-title":"Protein Eng."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1007\/s10856-010-4215-1","article-title":"In vivo effects of isolated implantation of salmon-derived crosslinked atelocollagen sponge into an osteochondral defect","volume":"22","author":"Kawaguchi","year":"2011","journal-title":"J. Mater. Sci. Mater. Med."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1002\/bab.1297","article-title":"High-level secretory expression and purification of unhydroxylated human collagen \u03b11 (III) chain in Pichia pastoris GS115","volume":"62","author":"Li","year":"2015","journal-title":"Biotechnol. Appl. Biochem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1002\/bab.1264","article-title":"New strategy for expression of recombinant hydroxylated human collagen alpha1(III) chains in Pichia pastoris GS115","volume":"62","author":"He","year":"2015","journal-title":"Biotechnol. Appl. Biochem."},{"key":"ref_41","unstructured":"Shi, J. (2017). Fermentation, Purification of Human Type III Collagen \u03b11 Chain and Construction of Hydroxylated \u03b11 Chain System. [Doctoral Dissertation, Northwest University]."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Zhang, Z., Li, J., Chen, Z., Du, H., Xia, W., Wang, Y., and Yu, H. (2025). Expression and Identification of a Novel High-Activity Recombinant Humanized Type I Collagen SynthCol1 in Pichia Pastoris. Res. Artic.","DOI":"10.21203\/rs.3.rs-7985426\/v1"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"rbad106","DOI":"10.1093\/rb\/rbad106","article-title":"Status and developmental trends in recombinant collagen preparation technology","volume":"11","author":"Guo","year":"2024","journal-title":"Regen. Biomater."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/j.nbt.2012.11.010","article-title":"Regulation of Pichia pastoris promoters and its consequences for protein production","volume":"30","author":"Vogl","year":"2013","journal-title":"New Biotechnol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"012039","DOI":"10.1088\/1755-1315\/217\/1\/012039","article-title":"Effect of IPTG concentration on recombinant human prethrombin-2 expression in E. coli BL21(DE3) arctic express","volume":"217","author":"Silaban","year":"2019","journal-title":"IOP Conf. Ser. Earth Environ. Sci."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Hausjell, J., Kutscha, R., Gesson, J.D., Reinisch, D., and Spadiut, O. (2020). The effects of lactose induction on a plasmid free E. coli T7 expression system. Bioengineering, 7.","DOI":"10.3390\/bioengineering7010008"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1007\/s00253-025-13566-3","article-title":"Efficient secretory expression of type III recombinant human collagen with triple-helical structure in Komagataella phaffii","volume":"109","author":"Ma","year":"2025","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_48","unstructured":"Cai, S.Z. (2022). Optimization of Recombinant Expression and Property Research of Human Type III Collagen in Pichia pastoris. [Doctoral Dissertation, South China University of Technology]."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1007\/s00253-010-2944-1","article-title":"Understanding the effect of foreign gene dosage on the physiology of Pichia pastoris by transcriptional analysis of key genes","volume":"89","author":"Zhu","year":"2011","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1186\/1475-2859-7-11","article-title":"Protein folding and conformational stress in microbial cells producing recombinant proteins: A host comparative overview","volume":"7","author":"Gasser","year":"2008","journal-title":"Microb. Cell Fact."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"114753","DOI":"10.1016\/j.lwt.2023.114753","article-title":"Increasing gene dosage and chaperones co-expression facilitate the efficient dextranase expression in Pichia pastoris","volume":"181","author":"Liu","year":"2023","journal-title":"LWT"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"5893","DOI":"10.1007\/s00253-022-12139-y","article-title":"Pathway engineering facilitates efficient protein expression in Pichia pastoris","volume":"106","author":"Liu","year":"2022","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"144270","DOI":"10.1016\/j.ijbiomac.2025.144270","article-title":"High-level secretory expression of recombinant type III human-like collagen \u03b11 in Pichia pastoris via multilevel systematic optimization","volume":"313","author":"Wang","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1016\/j.biortech.2017.05.105","article-title":"High level expression of recombinantthermostable \u03b2-glucosidase in E. coli by regulating acetic acid","volume":"241","author":"Shi","year":"2017","journal-title":"Bioresour. Technol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1002\/bab.1171","article-title":"Enhancing human-like collagen accumulation by deleting the major glucose transporter ptsG in recombinant E. coli BL21","volume":"61","author":"Luo","year":"2014","journal-title":"Biotechnol. Appl. Biochem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2567","DOI":"10.1021\/acssynbio.4c00345","article-title":"Biosynthesis of a functional fragment of human collagen II in Pichia pastoris","volume":"13","author":"Wang","year":"2024","journal-title":"ACS Synth. Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"131954","DOI":"10.1016\/j.ijbiomac.2024.131954","article-title":"An engineered Pichia pastoris platform for the biosynthesis of silk-based nanomaterials with therapeutic potential","volume":"269","author":"Tian","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S1004-9541(08)60334-1","article-title":"Optimization of fermentation process for human-like collagen production of recombinant E. coli using response surface methodology","volume":"18","author":"Zhang","year":"2010","journal-title":"Chin. J. Chem. Eng."},{"key":"ref_59","unstructured":"Liu, B. (2012). High-Density Fermentation Expression of Recombinant Human Collagen by Genetically Engineered Pichia pastoris. [Doctoral Dissertation, Nanjing University of Science and Technology]."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"6761","DOI":"10.1038\/s41467-022-34127-6","article-title":"Design of synthetic collagens that assemble into supramolecular banded fibers as a functional biomaterial testbed","volume":"13","author":"Hu","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"18537","DOI":"10.1074\/jbc.M110.112904","article-title":"Type III collagen, a fibril network modifier in articular cartilage","volume":"285","author":"Wu","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1018","DOI":"10.1016\/j.bbrc.2018.12.018","article-title":"Characterization by high-resolution crystal structure analysis of a triple-helix region of human collagen type III with potent cell adhesion activity","volume":"508","author":"Hua","year":"2019","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"131886","DOI":"10.1016\/j.ijbiomac.2024.131886","article-title":"Expression, characterization and antivascular activity of amino acid sequence repeating collagen hexadecapeptide","volume":"270","author":"Yan","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1042\/EBC20180053","article-title":"Role of prolyl hydroxylation in the molecular interactions of collagens","volume":"63","author":"Rappu","year":"2019","journal-title":"Essays Biochem."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"137400","DOI":"10.1016\/j.ijbiomac.2024.137400","article-title":"Optimizing prolyl hydroxylation for functional recombinant collagen in E. coli","volume":"282","author":"Zhu","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"147219","DOI":"10.1016\/j.ijbiomac.2025.147219","article-title":"Y326: A highly stable and bioactive substitute for animal-derived collagens in biomedical and cosmetic uses","volume":"323","author":"Deng","year":"2025","journal-title":"Int. J. Biol. Macromol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/6\/2563\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,3,13]],"date-time":"2026-03-13T05:23:24Z","timestamp":1773379404000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/6\/2563"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,3,11]]},"references-count":66,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2026,3]]}},"alternative-id":["ijms27062563"],"URL":"https:\/\/doi.org\/10.3390\/ijms27062563","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,3,11]]}}}