Biophysical Society Conference | Tahoe 2024

Molecular Biophysics of Membranes

Poster Abstracts

25-POS Board 7 INCREASING THE ENZYME ACTIVITY AND STABILITY BY CONTROLLING THE MEMBRANE COMPOSITION. Reza Razeghifard 1 ; Rachel Gruboy 1 ; Kena Patel 1 ; 1 Nova Southeastern University, Chemistry and Physics, Fort Lauderdale, FL, USA The purpose of this study is to make membrane assemblies capable of increasing and maintaining the catalytic activity of enzymes. Cytochrome P450 (CYP) and Carbonic anhydrase are the two enzymes studied here. CYP enzymes are responsible for the metabolism of a variety of drugs. This enzyme versatility in the choice of substrates can be beneficial since it can show if the new membrane assembly can indeed increase the enzyme activity/stability in the presence of different substrates. The enzyme activity is tested by detecting and quantifying the product concentrations using LCMS and GCMS depending on the product volatility. Butylated Hydroxytoluene (BHT) was used as the control substrate since it has a high affinity for the CYP enzyme. The most common products are hydroxylated substrates. However, the enzyme also produces hydrogen peroxide when the reaction is uncoupled. The coupling can be about 5% meaning that 95% of reduced NADP is wasted by the CYP as hydrogen peroxide. The CYP enzyme can then gradually lose its activity over time even under mild reaction conditions. Carbonic anhydrase is responsible for converting carbon dioxide into bicarbonate. The enzyme rapidly performs the reaction but the enzyme stability plays a key role in employing this enzyme for CO2 storage and capture since the reaction needs to be carried out at elevated temperatures. The enzyme activity can be measured spectrophotometrically by detecting a color compound produced by the esterase reaction.


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