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Efficient secretory expression of type III recombinant human collagen with triple-helical structure in Komagataella phaffii.

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Title: Efficient secretory expression of type III recombinant human collagen with triple-helical structure in Komagataella phaffii.
Authors: Ma, Yaqian1,2 (AUTHOR) mayaqian2017@163.com, Li, Yang3 (AUTHOR) liyang.0311@foxmail.com, Wang, Nan1,2 (AUTHOR) wangn121399@163.com, Han, Chenxiao1,2 (AUTHOR) hancx1121@163.com, Liu, Qisheng4 (AUTHOR) liuqs@zhbio.com, Sun, Liqin1,2 (AUTHOR) sliqin2005@163.com, Ma, Zhuqing5 (AUTHOR) mazhuqing@boan-bio.com, Zhang, Hailing1,2 (AUTHOR) hailing1203@hotmail.com
Source: Applied Microbiology & Biotechnology. 9/3/2025, Vol. 109 Issue 1, p1-17. 17p.
Subjects: Collagen, Helical structure, Production increases, Industrial applications, Proline hydroxylase, Pichia pastoris, Pharmaceutical technology
Abstract: Recombinant human collagen (rhCol) holds broad potential in biomedical and industrial applications due to its high purity and low immunogenicity. However, large-scale production of structurally stable and functionally active rhCol remains challenging. A novel strategy integrating collagen sequence optimization and microbial prolyl-4-hydroxylase (P4H) screening was developed to enable efficient production of triple-helical rhCol in Komagataella phaffii. Five Type III collagen variants (ColP1 ~ ColP5) were rationally designed based on interchain salt-bridge engineering to improve structural stability and biological activity, with ColP2 showing superior expression and functionality. A systematic evaluation of four microbial P4Hs identified Bacillus megaterium P4H (BmP4H) as the most effective catalyst for proline hydroxylation, enabling stable triple-helix formation. Combined with strain optimization, promoter and signal peptide screening, and 5-L scale fermentation, this approach achieved a high rhCol yield of 2.54 g/L with confirmed triple-helical structure. These results demonstrate an integrated and scalable platform for high-level production of functional recombinant collagen, providing a promising foundation for its industrial and clinical applications. Key Points • Co-expression of BmP4H enables stable triple-helical collagen in yeast. • Strain X-33, promoter PAOX1, and a-factor leader optimize collagen secretion. • Scale-up in 5L bioreactor achieves 2.54 g/L rhCol production. [ABSTRACT FROM AUTHOR]
Copyright of Applied Microbiology & Biotechnology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Efficient secretory expression of type III recombinant human collagen with triple-helical structure in Komagataella phaffii.
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  Data: <searchLink fieldCode="AR" term="%22Ma%2C+Yaqian%22">Ma, Yaqian</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<i> mayaqian2017@163.com</i><br /><searchLink fieldCode="AR" term="%22Li%2C+Yang%22">Li, Yang</searchLink><relatesTo>3</relatesTo> (AUTHOR)<i> liyang.0311@foxmail.com</i><br /><searchLink fieldCode="AR" term="%22Wang%2C+Nan%22">Wang, Nan</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<i> wangn121399@163.com</i><br /><searchLink fieldCode="AR" term="%22Han%2C+Chenxiao%22">Han, Chenxiao</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<i> hancx1121@163.com</i><br /><searchLink fieldCode="AR" term="%22Liu%2C+Qisheng%22">Liu, Qisheng</searchLink><relatesTo>4</relatesTo> (AUTHOR)<i> liuqs@zhbio.com</i><br /><searchLink fieldCode="AR" term="%22Sun%2C+Liqin%22">Sun, Liqin</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<i> sliqin2005@163.com</i><br /><searchLink fieldCode="AR" term="%22Ma%2C+Zhuqing%22">Ma, Zhuqing</searchLink><relatesTo>5</relatesTo> (AUTHOR)<i> mazhuqing@boan-bio.com</i><br /><searchLink fieldCode="AR" term="%22Zhang%2C+Hailing%22">Zhang, Hailing</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<i> hailing1203@hotmail.com</i>
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  Data: <searchLink fieldCode="JN" term="%22Applied+Microbiology+%26+Biotechnology%22">Applied Microbiology & Biotechnology</searchLink>. 9/3/2025, Vol. 109 Issue 1, p1-17. 17p.
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  Data: <searchLink fieldCode="DE" term="%22Collagen%22">Collagen</searchLink><br /><searchLink fieldCode="DE" term="%22Helical+structure%22">Helical structure</searchLink><br /><searchLink fieldCode="DE" term="%22Production+increases%22">Production increases</searchLink><br /><searchLink fieldCode="DE" term="%22Industrial+applications%22">Industrial applications</searchLink><br /><searchLink fieldCode="DE" term="%22Proline+hydroxylase%22">Proline hydroxylase</searchLink><br /><searchLink fieldCode="DE" term="%22Pichia+pastoris%22">Pichia pastoris</searchLink><br /><searchLink fieldCode="DE" term="%22Pharmaceutical+technology%22">Pharmaceutical technology</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Recombinant human collagen (rhCol) holds broad potential in biomedical and industrial applications due to its high purity and low immunogenicity. However, large-scale production of structurally stable and functionally active rhCol remains challenging. A novel strategy integrating collagen sequence optimization and microbial prolyl-4-hydroxylase (P4H) screening was developed to enable efficient production of triple-helical rhCol in Komagataella phaffii. Five Type III collagen variants (ColP1 ~ ColP5) were rationally designed based on interchain salt-bridge engineering to improve structural stability and biological activity, with ColP2 showing superior expression and functionality. A systematic evaluation of four microbial P4Hs identified Bacillus megaterium P4H (BmP4H) as the most effective catalyst for proline hydroxylation, enabling stable triple-helix formation. Combined with strain optimization, promoter and signal peptide screening, and 5-L scale fermentation, this approach achieved a high rhCol yield of 2.54 g/L with confirmed triple-helical structure. These results demonstrate an integrated and scalable platform for high-level production of functional recombinant collagen, providing a promising foundation for its industrial and clinical applications. Key Points • Co-expression of BmP4H enables stable triple-helical collagen in yeast. • Strain X-33, promoter PAOX1, and a-factor leader optimize collagen secretion. • Scale-up in 5L bioreactor achieves 2.54 g/L rhCol production. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Applied Microbiology & Biotechnology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1007/s00253-025-13566-3
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        Text: English
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      – SubjectFull: Collagen
        Type: general
      – SubjectFull: Helical structure
        Type: general
      – SubjectFull: Production increases
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      – SubjectFull: Industrial applications
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      – SubjectFull: Proline hydroxylase
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      – SubjectFull: Pichia pastoris
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      – SubjectFull: Pharmaceutical technology
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              Text: 9/3/2025
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