Utilizing Inductively Coupled Plasma Mass Spectrometry (ICP-MS) to Identify Metal Cofactors in PahZ2 Homologs
Faculty Mentor
Mitch Weiland
Location
Savannah Ballroom
Type of Research
On-going
Session Format
Poster Presentation
College
College of Science & Mathematics
Department
Department of Biochemistry, Chemistry, and Physics
Abstract
Poly(carboxylates) are water-soluble, synthetic polymers used in common, everyday products, such as detergents and diapers. These polymers are poorly biodegradable, and their accumulation can lead to detrimental environmental effects. Poly(aspartic acid) (PAA) has emerged as a naturally occurring, biodegradable alternative. To date, there are only three enzymes known to biodegrade PAA. Two of these enzymes cleave PAA into the smaller oligo(aspartic acid) (OAA), which is subsequently cleaved by PahZ2 from sphingomonas sp. KT-1 (PahZ2KT-1). PahZ2KT-1 is a metallo-exopeptidase, which harbors two Zn(II) atoms in its catalytic active site, and functions to liberate monomeric aspartic acid from OAA. Through bioinformatics searches, we have identified additional putative PahZ2 homologs. Given PahZ2KT-1 is the only known PAA exopeptidase, we aim to determine if these newly identified homologs also contain zinc in their active site. Here we will describe our method and preliminary results using inductively coupled plasma mass spectrometry (ICP-MS) to identify metal cofactors present in our PahZ2 homologs.
Program Description
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Start Date
4-21-2026 1:30 PM
End Date
4-21-2026 3:30 PM
Recommended Citation
Black, Taryn and Bechtel, Ken, "Utilizing Inductively Coupled Plasma Mass Spectrometry (ICP-MS) to Identify Metal Cofactors in PahZ2 Homologs" (2026). GS4 Student Scholars Symposium. 64.
https://digitalcommons.georgiasouthern.edu/research_symposium/2026A/2026A/64
Utilizing Inductively Coupled Plasma Mass Spectrometry (ICP-MS) to Identify Metal Cofactors in PahZ2 Homologs
Savannah Ballroom
Poly(carboxylates) are water-soluble, synthetic polymers used in common, everyday products, such as detergents and diapers. These polymers are poorly biodegradable, and their accumulation can lead to detrimental environmental effects. Poly(aspartic acid) (PAA) has emerged as a naturally occurring, biodegradable alternative. To date, there are only three enzymes known to biodegrade PAA. Two of these enzymes cleave PAA into the smaller oligo(aspartic acid) (OAA), which is subsequently cleaved by PahZ2 from sphingomonas sp. KT-1 (PahZ2KT-1). PahZ2KT-1 is a metallo-exopeptidase, which harbors two Zn(II) atoms in its catalytic active site, and functions to liberate monomeric aspartic acid from OAA. Through bioinformatics searches, we have identified additional putative PahZ2 homologs. Given PahZ2KT-1 is the only known PAA exopeptidase, we aim to determine if these newly identified homologs also contain zinc in their active site. Here we will describe our method and preliminary results using inductively coupled plasma mass spectrometry (ICP-MS) to identify metal cofactors present in our PahZ2 homologs.
