Development of: A Bacterial System for the Production of Hydroxylated Proteins en
Stanford bioengineers have developed a new E. coli system for the post-translational hydroxylation of recombinant proteins. Until now, this post-translational modification was only possible in higher organisms (such as yeast, mammalian or plant systems), which are much more expensive and difficult to work with than bacteria. Using an E. coli strain with a biosynthetic shunt to produce ascorbate-like molecules, this system can produce recombinant proteins with variable levels of hydroxylated proline residues. This technology could be employed in basic research to study hydroxylated proteins. Additionally, it has applications as part of a bacterial manufacturing system to produce inexpensive recombinant collagen, gelatins, or elastins for therapeutic or cosmetic uses. [ - ]
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- Development of: A Bacterial System for the Production of Hydroxylated Proteins
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- Stanford bioengineers have developed a new E. coli system for the post-translational hydroxylation of recombinant proteins. Until now, this post-translational modification was only possible in higher organisms (such as yeast, mammalian or plant systems), which are much more expensive and difficult to work with than bacteria. Using an E. coli strain with a biosynthetic shunt to produce ascorbate-like molecules, this system can produce recombinant proteins with variable levels of hydroxylated proline residues. This technology could be employed in basic research to study hydroxylated proteins. Additionally, it has applications as part of a bacterial manufacturing system to produce inexpensive recombinant collagen, gelatins, or elastins for therapeutic or cosmetic uses.
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