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Likewise, their random chain behaviour in physiological solution results in a strongly expanded hydrodynamic volume. Thus, apart from their use as fusion partner for biopharmaceuticals to achieve prolonged half-life in vivo, PAS biopolymers appear attractive as substitute for PEG\u2014or other poorly degradable chemical polymers\u2014in many areas. As a prerequisite for the wide application of PAS biopolymers at affordable cost, we have established their highly efficient biotechnological production in <jats:italic>Corynebacterium glutamicum<\/jats:italic> serving as a well characterized bacterial host organism.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Results<\/jats:title>\n                <jats:p>Using the CspA signal sequence, we have secreted two representative PAS biopolymers as polypeptides with\u2009~\u2009600 and\u2009~\u20091200 amino acid residues, respectively. Both PAS biopolymers were purified from the culture supernatant by means of a simple downstream process in a truly\u00a0monodisperse state as evidenced by ESI\u2013MS. Yields after purification were up to\u2009\u2265\u20094\u00a0g per liter culture, with potential for further increase by strain optimization as well as fermentation and bioprocess development. Beyond direct application as hydrocolloids or to exploit their rheological properties, such PAS biopolymers are suitable for site-specific chemical conjugation with pharmacologically active molecules via their unique terminal amino or carboxyl groups. To enable the specific activation of the carboxylate, without interference by the free amino group, we generated a blocked N-terminus for the PAS(1200) polypeptide simply by introducing an N-terminal Gln residue which, after processing of the signal peptide, was cyclised to a chemically\u00a0inert pyroglutamyl group upon acid treatment. The fact that PAS biopolymers are genetically encoded offers further conjugation strategies via incorporation of amino acids with reactive side chains (e.g., Cys, Lys, Glu\/Asp) at defined positions.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Conclusions<\/jats:title>\n                <jats:p>Our new PAS expression platform using Corynex<jats:sup>\u00ae<\/jats:sup> technology opens the way to applications of PASylation<jats:sup>\u00ae<\/jats:sup> technology in multiple areas such as the pharmaceutical industry, cosmetics and food technology.<\/jats:p>\n              <\/jats:sec>","DOI":"10.1186\/s12934-022-01948-5","type":"journal-article","created":{"date-parts":[[2022,10,28]],"date-time":"2022-10-28T21:02:41Z","timestamp":1666990961000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Efficient secretory production of proline\/alanine\/serine (PAS) biopolymers in Corynebacterium glutamicum yielding a monodisperse biological alternative to polyethylene glycol (PEG)"],"prefix":"10.1186","volume":"21","author":[{"given":"L.","family":"Friedrich","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Y.","family":"Kikuchi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Y.","family":"Matsuda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"U.","family":"Binder","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.","family":"Skerra","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2022,10,28]]},"reference":[{"key":"1948_CR1","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-7643-8679-5","volume-title":"PEGylated protein drugs: basic science and clinical applications","author":"FM Veronese","year":"2009","unstructured":"Veronese FM. 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