Area of Study
Science and Mathematics
Sequencing of the HD100 genome of Bdellovibrio Bacteriovorus in 2005 revealed a gene for the putative maltase, MalA. However, given the bacterium’s observed disuse of prey carbohydrates as an energy source, this enzyme is seemingly out of place. In this study, the specificity and activity of MalA were explored through various enzymatic assays. Using p-nitrophenol-α-D-glucopyranoside (p-NPG) as a colorimetric substrate to allow for rapid and accurate detection of enzymatic activity through spectrophotometry, enzyme stability inhibition of p-NPG cleavage were explored. While numerous alpha-linked disaccharides were shown to inhibit MalA, only maltose was shown to be cleaved into glucose.
Isabella, Christine, "Exploration of the active site specificity of MalA, a glucosidase from the predatory bacterium Bdellovibrio bacteriovorus" (2011). Summer Research. 107.
University of Puget Sound