Asset Details
Do you wish to reserve the book?
Efficient secretory expression of type III recombinant human collagen with triple-helical structure in Komagataella phaffii
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Efficient secretory expression of type III recombinant human collagen with triple-helical structure in Komagataella phaffii
Do you wish to request the book?
Efficient secretory expression of type III recombinant human collagen with triple-helical structure in Komagataella phaffii
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Efficient secretory expression of type III recombinant human collagen with triple-helical structure in Komagataella phaffii
2025
Overview
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 P
AOX1
, and a-factor leader optimize collagen secretion.
•
Scale-up in 5L bioreactor achieves 2.54 g/L rhCol production.
Publisher
Springer Berlin Heidelberg,Springer Nature B.V,Springer
Subject
/ Biomedical and Life Sciences
/ Bridges
/ Collagen
/ Collagen Type III - biosynthesis
/ Collagen Type III - chemistry
/ Collagen Type III - genetics
/ Collagen Type III - metabolism
/ Design
/ Enzymes
/ Humans
/ Microbial Genetics and Genomics
/ Peptides
/ proline
/ Prolyl Hydroxylases - genetics
/ Prolyl Hydroxylases - metabolism
/ Proteins
/ Recombinant Proteins - biosynthesis
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Saccharomycetales - genetics
/ Saccharomycetales - metabolism
/ Yeast
/ yeasts
