Presenter(s)

    Katelyn Beavan

    Comments

    1:15-2:30, Kennedy Union Ballroom

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    Description

    Lactate dehydrogenase (LDH) plays a crucial role in cellular metabolism. It converts pyruvate to lactic acid, which subsequently lowers pH. This study examines how propionate influences LDH activity and pH under anaerobic conditions in wild-type (WT) and mutant bacterial strains. Specifically, I analyze the effects of propionate on WT, ∆codY, and ∆sigB mutants of Listeria monocytogenes to determine how these genetic modifications alter metabolic responses. My methodology involved culturing WT and mutant strains in brain heart infusion (BHI) media with and without 25 mM propionate. The samples were incubated at 37°C under aerobic and anaerobic conditions for 20 hours. By measuring pH changes, we assessed how propionate affects LDH activity in different genetic backgrounds. Preliminary results indicate that the presence of propionate alters pH levels in both WT and mutant strains, suggesting its impact on LDH function. I hope to further understand these metabolic interactions and provide insight into bacterial adaptation and survival. Future work will focus on further characterizing these effects and continue to establish how propionate effects the microbial metabolism.

    Publication Date

    4-23-2025

    Project Designation

    Independent Research

    Primary Advisor

    Yvonne Y. Sun

    Primary Advisor's Department

    Biology

    Keywords

    Stander Symposium, College of Arts and Sciences

    Institutional Learning Goals

    Practical Wisdom; Vocation; Community

    Anaerobic Propionate and pH: Investigating LDH Activity in Mutants

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