{"id":{"repo_id":"unr","oai_identifier":"oai:scholarwolf.unr.edu:11714/626"},"canonical_url":"https://search.dev.ndltd.org/etd/unr/oai:scholarwolf.unr.edu:11714/626","repository":{"repo_id":"unr","name":"University of Nevada - Reno","base_url":"https://scholarwolf.unr.edu/server/oai/request"},"display":{"title":"Characterization and Heterologous Expression of Recombinant Drosophila melanogaster Fatty Acyl CoA Reductase","abstract":"Insect genomes have multiple fatty acyl CoA reductases (FARs), which implies varying substrate and product profiles. However, very few of these FARs have been characterized. Expression of the FAR CG18031 from Drosophila melanogaster in Spodoptera frugiperda (Sf)9 cells will allow for functional characterization of the enzyme. Substrate and chain-length specificity can then be determined by gas chromatography analysis. Results from the functional characterization will provide a greater insight into the biochemistry of insect hydrocarbon synthesis. This information can be used to implement insect FARs into a plant system for increased hydrocarbon production and more cost-efficient biofuels.","abstract_html":"Insect genomes have multiple fatty acyl CoA reductases (FARs), which implies varying substrate and product profiles. However, very few of these FARs have been characterized. Expression of the FAR CG18031 from Drosophila melanogaster in Spodoptera frugiperda (Sf)9 cells will allow for functional characterization of the enzyme. Substrate and chain-length specificity can then be determined by gas chromatography analysis. Results from the functional characterization will provide a greater insight into the biochemistry of insect hydrocarbon synthesis. This information can be used to implement insect FARs into a plant system for increased hydrocarbon production and more cost-efficient biofuels.","abstract_has_math":false,"creators":["Nowinski, Magda"],"institution":"University of Nevada, Reno","degree_name":"Biochem and Molecular Biology","degree_level":"Honors Thesis","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Tittiger, Claus R."],"committee_chairs":[],"committee_members":[],"year":2012,"date_issued":"2012","date_published":"2012","updated_at":"2026-07-27T21:47:25Z","subjects":[],"languages":["en_US","English"],"rights":["In Copyright(All Rights Reserved)"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/11714/626","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Tittiger, Claus R."]},{"key":"dc:creator","label":"Author","values":["Nowinski, Magda"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2017-01-24T23:09:17Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2017-01-24T23:09:17Z"]},{"key":"dc:date.issued","label":"Date","values":["2012"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Honors Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Biochem and Molecular Biology"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Nevada, Reno"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English"]},{"key":"dc:language.iso","label":"Language (ISO)","values":["en_US"]},{"key":"dc:rights","label":"Dc Rights","values":["In Copyright(All Rights Reserved)"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/11714/626"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The University of Nevada, Reno Libraries will promptly respond to removal requests related to content that violates intellectual property laws, data protections, or has been uploaded without creator consent. Takedown notices should be directed to our ScholarWolf team (scholarwolf@library.unr.edu) with information about the object, including its full URL and the nature of your complaint."]},{"key":"dc:description.abstract","label":"Abstract","values":["Insect genomes have multiple fatty acyl CoA reductases (FARs), which implies varying substrate and product profiles. However, very few of these FARs have been characterized. Expression of the FAR CG18031 from Drosophila melanogaster in Spodoptera frugiperda (Sf)9 cells will allow for functional characterization of the enzyme. Substrate and chain-length specificity can then be determined by gas chromatography analysis. Results from the functional characterization will provide a greater insight into the biochemistry of insect hydrocarbon synthesis. This information can be used to implement insect FARs into a plant system for increased hydrocarbon production and more cost-efficient biofuels."]},{"key":"dc:format","label":"Dc Format","values":["PDF"]},{"key":"dc:title","label":"Title","values":["Characterization and Heterologous Expression of Recombinant Drosophila melanogaster Fatty Acyl CoA Reductase"]}]}],"canonical_facts":{"dc:contributor.advisor":["Tittiger, Claus R."],"dc:creator":["Nowinski, Magda"],"dc:date.accessioned":["2017-01-24T23:09:17Z"],"dc:date.available":["2017-01-24T23:09:17Z"],"dc:date.issued":["2012"],"dc:description":["The University of Nevada, Reno Libraries will promptly respond to removal requests related to content that violates intellectual property laws, data protections, or has been uploaded without creator consent. Takedown notices should be directed to our ScholarWolf team (scholarwolf@library.unr.edu) with information about the object, including its full URL and the nature of your complaint."],"dc:description.abstract":["Insect genomes have multiple fatty acyl CoA reductases (FARs), which implies varying substrate and product profiles. However, very few of these FARs have been characterized. Expression of the FAR CG18031 from Drosophila melanogaster in Spodoptera frugiperda (Sf)9 cells will allow for functional characterization of the enzyme. Substrate and chain-length specificity can then be determined by gas chromatography analysis. Results from the functional characterization will provide a greater insight into the biochemistry of insect hydrocarbon synthesis. This information can be used to implement insect FARs into a plant system for increased hydrocarbon production and more cost-efficient biofuels."],"dc:format":["PDF"],"dc:identifier.uri":["http://hdl.handle.net/11714/626"],"dc:language":["English"],"dc:language.iso":["en_US"],"dc:rights":["In Copyright(All Rights Reserved)"],"dc:title":["Characterization and Heterologous Expression of Recombinant Drosophila melanogaster Fatty Acyl CoA Reductase"],"dc:type":["Thesis"],"thesis:degree_level":["Honors Thesis"],"thesis:degree_name":["Biochem and Molecular Biology"],"thesis:institution_name":["University of Nevada, Reno"]},"updated_at":"2026-07-27T21:47:25Z"}