Date of Submission
Fall 2024
Academic Program
Division of Science, Mathematics, and Computing; Chemistry and Biochemistry
Project Advisor 1
Emily McLaughlin
Project Advisor 2
Swapan Jain
Abstract/Artist's Statement
New biocatalytic enzymes are being discovered and celebrated for their ability to lower reaction rates and yield high enantiomeric excess. Traditional chemical catalysis in synthetic chemistry often employs metals, many of which are dwindling on our planet, whereas enzymes and biological organisms, which are regenerative and accessible, are worthy alternatives to metal catalysis. In this work, we focus on the acyltransferase enzyme from Mycobacterium smegmatis (MsAct). MsAct has been shown to favor condensation reactions over hydrolysis in aqueous conditions due to its hydrophobic pocket, making it a promising candidate for a wide range of industrial applications. The enzyme has been previously reported to perform trans-esterification, amidation, trans-amidation, and per hydrolysis reactions exceptionally well, and can withstand a wide range of pH (6-10) environments compared to that of other known biocatalysts. Previous studies have also reported MsAct’s performance of the reverse reaction, specifically hydrolysis of the newly formed ester product, after prolonged reaction times, highlighting its dynamic catalytic capabilities. Herein this study explores the relationship between MsAct concentration to perform acetylation reactions, as well as exploring MsAct’s enantioselectivity and its activity towards more polar substrates.
Open Access Agreement
On-Campus only
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
Recommended Citation
Malick, Gwenn, "Exploring the catalytic power of acyltransferase from Mycobacterium Smegmatis" (2024). Senior Projects Fall 2024. 52.
https://digitalcommons.bard.edu/senproj_f2024/52
This work is protected by a Creative Commons license. Any use not permitted under that license is prohibited.
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