Title |
Use of Nanostructure-Initiator Mass Spectrometry to Deduce Selectivity of Reaction in Glycoside Hydrolases
|
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Published in |
Frontiers in Bioengineering and Biotechnology, October 2015
|
DOI | 10.3389/fbioe.2015.00165 |
Pubmed ID | |
Authors |
Kai Deng, Taichi E. Takasuka, Christopher M. Bianchetti, Lai F. Bergeman, Paul D. Adams, Trent R. Northen, Brian G. Fox |
Abstract |
Chemically synthesized nanostructure-initiator mass spectrometry (NIMS) probes derivatized with tetrasaccharides were used to study the reactivity of representative Clostridium thermocellum β-glucosidase, endoglucanases, and cellobiohydrolase. Diagnostic patterns for reactions of these different classes of enzymes were observed. Results show sequential removal of glucose by the β-glucosidase and a progressive increase in specificity of reaction from endoglucanases to cellobiohydrolase. Time-dependent reactions of these polysaccharide-selective enzymes were modeled by numerical integration, which provides a quantitative basis to make functional distinctions among a continuum of naturally evolved catalytic properties. Consequently, our method, which combines automated protein translation with high-sensitivity and time-dependent detection of multiple products, provides a new approach to annotate glycoside hydrolase phylogenetic trees with functional measurements. |
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