{"id":{"repo_id":"ttu","oai_identifier":"oai:ttu-ir.tdl.org:2346/97430"},"canonical_url":"https://search.dev.ndltd.org/etd/ttu/oai:ttu-ir.tdl.org:2346/97430","repository":{"repo_id":"ttu","name":"Texas Technology University","base_url":"https://ttu-ir.tdl.org/server/oai/request"},"display":{"title":"Bioaffinity-based Concept for Glyphosate Detection","abstract":"In recent decades, there has been a growing emphasis on improving investigation capacities in the field of forensic toxicology. This study looks into the interaction between acetylcholinesterase (AChE) and glyphosate, specifically its potential suppression. The study optimizes parameters such as pH levels, enzyme concentrations, and substrate concentrations using the Ellman enzymatic assay. AChE activity is best maintained at 50 mU with 3 mM DTNB and 5 mM ACth, and storage at 4°C assures stability. The study also exposes glyphosate's inhibitory effect on AChE, demonstrating its potential hazards to human health and the environment. Comparisons with butyrylcholinesterase (BChE) demonstrate each enzyme's distinct stability and selectivity. These findings shed light on the complex interactions between glyphosate and cholinesterase, paving the path for breakthroughs in toxicology and related sciences.","abstract_html":"In recent decades, there has been a growing emphasis on improving investigation capacities in the field of forensic toxicology. This study looks into the interaction between acetylcholinesterase (AChE) and glyphosate, specifically its potential suppression. The study optimizes parameters such as pH levels, enzyme concentrations, and substrate concentrations using the Ellman enzymatic assay. AChE activity is best maintained at 50 mU with 3 mM DTNB and 5 mM ACth, and storage at 4°C assures stability. The study also exposes glyphosate's inhibitory effect on AChE, demonstrating its potential hazards to human health and the environment. Comparisons with butyrylcholinesterase (BChE) demonstrate each enzyme's distinct stability and selectivity. These findings shed light on the complex interactions between glyphosate and cholinesterase, paving the path for breakthroughs in toxicology and related sciences.","abstract_has_math":false,"creators":["Haddock, Elizabeth (Lissa)"],"institution":"Texas Tech University","degree_name":"Master of Science","degree_level":"Masters","degree_discipline":"Forensic Science","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":["Halamek, Jan"],"committee_members":["Ramkumar, S. 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This study looks into the interaction between acetylcholinesterase (AChE) and glyphosate, specifically its potential suppression. The study optimizes parameters such as pH levels, enzyme concentrations, and substrate concentrations using the Ellman enzymatic assay. AChE activity is best maintained at 50 mU with 3 mM DTNB and 5 mM ACth, and storage at 4°C assures stability. The study also exposes glyphosate's inhibitory effect on AChE, demonstrating its potential hazards to human health and the environment. Comparisons with butyrylcholinesterase (BChE) demonstrate each enzyme's distinct stability and selectivity. These findings shed light on the complex interactions between glyphosate and cholinesterase, paving the path for breakthroughs in toxicology and related sciences.","Embargo status: Restricted until 01/2027. To request the author grant access, click on the PDF link to the left."]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["Application/pdf"]},{"key":"dc:title","label":"Title","values":["Bioaffinity-based Concept for Glyphosate Detection"]}]}],"canonical_facts":{"dc:contributor.committeechair":["Halamek, Jan"],"dc:contributor.committeemember":["Ramkumar, S. S.","Swed, Ori"],"dc:creator":["Haddock, Elizabeth (Lissa)"],"dc:date.accessioned":["2024-01-09T16:10:09Z"],"dc:date.available":["2024-01-09T16:10:09Z"],"dc:date.issued":["2023-12"],"dc:description.abstract":["In recent decades, there has been a growing emphasis on improving investigation capacities in the field of forensic toxicology. This study looks into the interaction between acetylcholinesterase (AChE) and glyphosate, specifically its potential suppression. The study optimizes parameters such as pH levels, enzyme concentrations, and substrate concentrations using the Ellman enzymatic assay. AChE activity is best maintained at 50 mU with 3 mM DTNB and 5 mM ACth, and storage at 4°C assures stability. The study also exposes glyphosate's inhibitory effect on AChE, demonstrating its potential hazards to human health and the environment. Comparisons with butyrylcholinesterase (BChE) demonstrate each enzyme's distinct stability and selectivity. These findings shed light on the complex interactions between glyphosate and cholinesterase, paving the path for breakthroughs in toxicology and related sciences.","Embargo status: Restricted until 01/2027. To request the author grant access, click on the PDF link to the left."],"dc:format.mimetype":["Application/pdf"],"dc:identifier.uri":["https://hdl.handle.net/2346/97430"],"dc:language.iso":["en"],"dc:subject":["acetylcholinesterase","organophosphate","glyphosate","enzymatic optimization","enzyme stability","glyphosate detection"],"dc:title":["Bioaffinity-based Concept for Glyphosate Detection"],"dc:type":["Thesis"],"thesis:degree_discipline":["Forensic Science"],"thesis:degree_level":["Masters"],"thesis:degree_name":["Master of Science"],"thesis:institution_name":["Texas Tech University"]},"updated_at":"2026-07-24T05:04:51Z"}