The evolution of cyclodextrin glucanotransferase product specificity |
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Authors: | Ronan M Kelly Lubbert Dijkhuizen Hans Leemhuis |
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Institution: | (1) Microbial Physiology, Groningen Biomolecular Sciences and Biotechnology Institute, Centre for Carbohydrate Bioprocessing, University of Groningen, Kerklaan 30, 9751 NN Haren, the Netherlands |
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Abstract: | Cyclodextrin glucanotransferases (CGTases) have attracted major interest from industry due to their unique capacity of forming
large quantities of cyclic α-(1,4)-linked oligosaccharides (cyclodextrins) from starch. CGTases produce a mixture of cyclodextrins
from starch consisting of 6 (α), 7 (β) and 8 (γ) glucose units. In an effort to identify the structural factors contributing
to the evolutionary diversification of product specificity amongst this group of enzymes, we selected nine CGTases from both
mesophilic, thermophilic and hyperthermophilic organisms for comparative product analysis. These enzymes displayed considerable
variation regarding thermostability, initial rates, percentage of substrate conversion and ratio of α-, β- and γ-cyclodextrins
formed from starch. Sequence comparison of these CGTases revealed that specific incorporation and/or substitution of amino
acids at the substrate binding sites, during the evolutionary progression of these enzymes, resulted in diversification of
cyclodextrin product specificity.
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users.
Hans Leemhuis acknowledges financial support from the Netherlands Organization for Scientific Research (NWO). |
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Keywords: | Protein evolution CGTase α -Amylase Reaction specificity Protein stability |
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