{"id":{"repo_id":"duke","oai_identifier":"oai:dukespace.lib.duke.edu:10161/20900"},"canonical_url":"https://search.dev.ndltd.org/etd/duke/oai:dukespace.lib.duke.edu:10161/20900","repository":{"repo_id":"duke","name":"Duke University","base_url":"https://dukespace.lib.duke.edu/server/oai/request"},"display":{"title":"Overcoming long-standing challenges in recombinant protein expression","abstract":"<p>The market for proteins has been constantly increasing for many different applications, such as protein-based drugs. However, protein production in E. coli, the most widely used recombinant host, has remained fundamentally the same since its inception. Here, we developed from the bottom up, a new expression platform using synthetic biology. The resulting platform reaches high protein titer across scales and allows for autoinduction and autolysis. More importantly, we are able to decouple growth from protein production and show that this platform is easily adaptable to other applications such as (i) reduction of essential housekeeping proteases to enable production of “hard-to-express” proteins and (ii) complete in vivo post-translational modifications.</p>","abstract_html":"&lt;p&gt;The market for proteins has been constantly increasing for many different applications, such as protein-based drugs. However, protein production in E. coli, the most widely used recombinant host, has remained fundamentally the same since its inception. Here, we developed from the bottom up, a new expression platform using synthetic biology. The resulting platform reaches high protein titer across scales and allows for autoinduction and autolysis. More importantly, we are able to decouple growth from protein production and show that this platform is easily adaptable to other applications such as (i) reduction of essential housekeeping proteases to enable production of “hard-to-express” proteins and (ii) complete in vivo post-translational modifications.&lt;/p&gt;","abstract_has_math":false,"creators":["Menacho Melgar, Romel"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Lynch, Michael D"],"committee_chairs":[],"committee_members":[],"year":2020,"date_issued":"2020","date_published":"2020","updated_at":"2026-07-24T02:06:56Z","subjects":["Biomedical engineering"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/10161/20900","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Lynch, Michael D"]},{"key":"dc:creator","label":"Author","values":["Menacho Melgar, Romel"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2020-06-09T17:58:45Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2022-05-27T08:17:09Z"]},{"key":"dc:date.issued","label":"Date","values":["2020"]},{"key":"dc:type","label":"Dc Type","values":["Dissertation"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biomedical engineering"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/10161/20900"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["<p>The market for proteins has been constantly increasing for many different applications, such as protein-based drugs. However, protein production in E. coli, the most widely used recombinant host, has remained fundamentally the same since its inception. Here, we developed from the bottom up, a new expression platform using synthetic biology. The resulting platform reaches high protein titer across scales and allows for autoinduction and autolysis. More importantly, we are able to decouple growth from protein production and show that this platform is easily adaptable to other applications such as (i) reduction of essential housekeeping proteases to enable production of “hard-to-express” proteins and (ii) complete in vivo post-translational modifications.</p>"]},{"key":"dc:title","label":"Title","values":["Overcoming long-standing challenges in recombinant protein expression"]}]}],"canonical_facts":{"dc:contributor.advisor":["Lynch, Michael D"],"dc:creator":["Menacho Melgar, Romel"],"dc:date.accessioned":["2020-06-09T17:58:45Z"],"dc:date.available":["2022-05-27T08:17:09Z"],"dc:date.issued":["2020"],"dc:description.abstract":["<p>The market for proteins has been constantly increasing for many different applications, such as protein-based drugs. However, protein production in E. coli, the most widely used recombinant host, has remained fundamentally the same since its inception. Here, we developed from the bottom up, a new expression platform using synthetic biology. The resulting platform reaches high protein titer across scales and allows for autoinduction and autolysis. More importantly, we are able to decouple growth from protein production and show that this platform is easily adaptable to other applications such as (i) reduction of essential housekeeping proteases to enable production of “hard-to-express” proteins and (ii) complete in vivo post-translational modifications.</p>"],"dc:identifier.uri":["https://hdl.handle.net/10161/20900"],"dc:subject":["Biomedical engineering"],"dc:title":["Overcoming long-standing challenges in recombinant protein expression"],"dc:type":["Dissertation"]},"updated_at":"2026-07-24T02:06:56Z"}