The unique and largely uncharacterized repertoire of proteolytic enzymes possessed by microbes offers a window into the metabolic lifestyle of these organisms, and their impacts on the global carbon cycle. Ascertaining the chemical identity of the numerous metalloproteases possessed by the ubiquitous marine heterotrophic bacterium, Alteromonas, allows for an understanding of the effects acidification on the trace metal requirements and function of these proteolytic enzymes. Proteomics, in tandem with trace metal analysis, can be used to assemble a picture of the metalloproteome, providing an unprecedented and full characterization of these metalloproteases. This work will detail the methods of purification by liquid chromatography, tandem mass spectrometry and inductively coupled plasma mass spectrometry (ICP-MS) employed to arrive at the characterization of the metalloproteome of Alteromonas. Additional discussion will focus on the effect of acidification on the proteolytic activities of these purified metalloproteins.

Characterization of the proteolytic enzymes of a marine bacterium, Alteromonas through metalloproteomics

2019 Spring National Meeting

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