PahZ1KT-1: Determining Thermodynamic Parameters of Enzyme-Substrate Interactions Using Isothermal Titration Calorimetry (ITC)
Faculty Mentor
Mitch Weiland
Location
Savannah Ballroom
Type of Research
On-going
Session Format
Poster Presentation
College
College of Science & Mathematics
Department
Biochemistry, Chemistry, and Physics
Abstract
Polycarboxylates are synthetic polymers that are useful for a number of applications, including in industrial water treatment systems and as antiscaling agents. Though of utility, these are not biodegradable, and there is concern these polymers may leech into and taint the water supply due to their water-soluble nature. Efforts to combat this have resulted in use of a greener alternative, poly(aspartic acid) (PAA), synthesized from naturally occurring L-aspartic acid. There are only three known enzymes, originating from the PahZ gene, capable of degrading PAA: PahZ1KT-1, PahZ2KT-1 and PahZ1KP-2. Previous efforts have determined PahZ1KT-1 to have DNA binding activity in addition to PAA hydrolysis activity. At present, efforts are being made to use isothermal titration calorimetry (ITC) to determine the thermodynamic parameters, including binding constants, reaction stoichiometry, enthalpy, and entropy to further characterize these enzyme-substrate interactions.
Program Description
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Start Date
4-21-2026 1:30 PM
End Date
4-21-2026 3:30 PM
Recommended Citation
Nguyen, Catherine T. and Lopez-Marquez, Morelia N., "PahZ1KT-1: Determining Thermodynamic Parameters of Enzyme-Substrate Interactions Using Isothermal Titration Calorimetry (ITC)" (2026). GS4 Student Scholars Symposium. 65.
https://digitalcommons.georgiasouthern.edu/research_symposium/2026A/2026A/65
PahZ1KT-1: Determining Thermodynamic Parameters of Enzyme-Substrate Interactions Using Isothermal Titration Calorimetry (ITC)
Savannah Ballroom
Polycarboxylates are synthetic polymers that are useful for a number of applications, including in industrial water treatment systems and as antiscaling agents. Though of utility, these are not biodegradable, and there is concern these polymers may leech into and taint the water supply due to their water-soluble nature. Efforts to combat this have resulted in use of a greener alternative, poly(aspartic acid) (PAA), synthesized from naturally occurring L-aspartic acid. There are only three known enzymes, originating from the PahZ gene, capable of degrading PAA: PahZ1KT-1, PahZ2KT-1 and PahZ1KP-2. Previous efforts have determined PahZ1KT-1 to have DNA binding activity in addition to PAA hydrolysis activity. At present, efforts are being made to use isothermal titration calorimetry (ITC) to determine the thermodynamic parameters, including binding constants, reaction stoichiometry, enthalpy, and entropy to further characterize these enzyme-substrate interactions.
