Evaluating the enzymatic degradation of oligo(aspartic acid) by a novel poly(aspartic acid) hydrolase
Faculty Mentor
Mitch H. Weiland
Location
Savannah Ballroom
Type of Research
On-going
Session Format
Poster Presentation
College
College of Science & Mathematics
Department
Biochemistry, Chemistry, & Physics
Abstract
Polymers are valuable for the number of utilities they offer, cementing their global presence. However, with their prevalence paired with their extended lifetime, polymers also pose a potential detriment to the environment. An emerging alternative to water-soluble non-biodegradable polymers is poly(aspartic acid) (PAA). This polymer is capable of a variety of industrial applications ranging from removal of metals in water to functioning as a superabsorbent material. The appeal of PAA lies in its derivation from a naturally occurring amino acid, aspartic acid, and its ability to be enzymatically degraded back to its monomeric form. Currently, there are only three enzymes reported to hydrolyze PAA. Their mechanism of biodegradation begins with PahZ1, from either the Sphingomonas sp. KT-1 (PahZ1 KT-1) or Pedobacter sp. KP-2 (PahZ1 KP-2), creating a diminished form of PAA, digested PAA (dPAA), which is subsequently acted upon by the second enzyme PahZ2 KT-1 to produce free aspartic acid. To date, only PahZ2 KT-1 is known to produce free aspartic acid. Using bioinformatic procedures, we have identified a second PahZ2 homolog capable of behaving in a similar fashion. Initial results support the potential of this newly identified enzyme as harboring dPAA degradation activity.
Program Description
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Start Date
4-21-2026 10:00 AM
End Date
4-21-2026 12:00 PM
Recommended Citation
Song, Samuel E., "Evaluating the enzymatic degradation of oligo(aspartic acid) by a novel poly(aspartic acid) hydrolase" (2026). GS4 Student Scholars Symposium. 18.
https://digitalcommons.georgiasouthern.edu/research_symposium/2026A/2026A/18
Evaluating the enzymatic degradation of oligo(aspartic acid) by a novel poly(aspartic acid) hydrolase
Savannah Ballroom
Polymers are valuable for the number of utilities they offer, cementing their global presence. However, with their prevalence paired with their extended lifetime, polymers also pose a potential detriment to the environment. An emerging alternative to water-soluble non-biodegradable polymers is poly(aspartic acid) (PAA). This polymer is capable of a variety of industrial applications ranging from removal of metals in water to functioning as a superabsorbent material. The appeal of PAA lies in its derivation from a naturally occurring amino acid, aspartic acid, and its ability to be enzymatically degraded back to its monomeric form. Currently, there are only three enzymes reported to hydrolyze PAA. Their mechanism of biodegradation begins with PahZ1, from either the Sphingomonas sp. KT-1 (PahZ1 KT-1) or Pedobacter sp. KP-2 (PahZ1 KP-2), creating a diminished form of PAA, digested PAA (dPAA), which is subsequently acted upon by the second enzyme PahZ2 KT-1 to produce free aspartic acid. To date, only PahZ2 KT-1 is known to produce free aspartic acid. Using bioinformatic procedures, we have identified a second PahZ2 homolog capable of behaving in a similar fashion. Initial results support the potential of this newly identified enzyme as harboring dPAA degradation activity.
