The enzyme ADH-A and one of its mutants ADH-A C1B1 from Rhodococcus ruber, have in previous studies been proved to act as proper biocatalysts, fully capable of performing redox reactions. Two redox reactions were studied during this project, were those enzymes act as catalysts. For that matter, ADH-A wild type and ADH-A C1B1 genes were expressed in E. coli and the encoded enzymes were purified and used for kinetic studies with a final goal on studying the kinetic isotope effect that is generated between them and the molecules that contain deuterium. HPLC analysis on these products showed that the reactions were not thermodynamically favored and conclusions on the best reaction conditions for both enzymes as well as for further improvements are discussed.
| Identifer | oai:union.ndltd.org:UPSALLA1/oai:DiVA.org:uu-368315 |
| Date | January 2018 |
| Creators | Serveta, Irena |
| Publisher | Uppsala universitet, Institutionen för kemi - BMC |
| Source Sets | DiVA Archive at Upsalla University |
| Language | English |
| Detected Language | English |
| Type | Student thesis, info:eu-repo/semantics/bachelorThesis, text |
| Format | application/pdf |
| Rights | info:eu-repo/semantics/openAccess |
| Relation | UPKEM C ; 128 |
Page generated in 0.0212 seconds