Isolation, Purification, and Characterization of Piscicosins V1a and V1b
Presenter
:
Ethan Ng
Co-Presenter(s)
:
Rachael Miller, Sophia Pettid
Presenter Status
:
Undergraduate student
Academic Year
:
20-21
Semester
:
Spring
Faculty Mentor
:
Monica Lares
Department
:
Chemistry
Presentation Link
:
Abstract
:
Class IIa bacteriocins are small, non-lantibiotic, ribosomally-synthesized, anti-listerial peptides with a conserved YGNGV motif in their N-Termini1. Piscicosins V1a and V1b are both endogenously generated by the bacteria Carnobacterium Piscicola (C. Pisc)1. Piscicosin V1a is 44 residues at 4,416 Da and Piscicosin V1b is 43 residues at 4,526 Da1. In these experiments, we have attempted to isolate both bacteriocins from C. Pisc, purify the crude product, and characterize its antimicrobial activity against Listeria Monocytogenes (L. Mono). Purification methods performed in this manuscript include solid-phase extraction and reverse-phase HPLC (RP-HPLC).