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  Mechanistic comparison of saccharide depolymerization catalyzed by dicarboxylic acids and glycosidases

Kayser, H., Rodríguez-Ropero, F., Leitner, W., Fioroni, M., & Domínguez de María, P. (2013). Mechanistic comparison of saccharide depolymerization catalyzed by dicarboxylic acids and glycosidases. RSC Advances, 3(24), 9273-9278. doi:10.1039/C3RA41307A.

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c3ra41307a.pdf (Supplementary material), 456KB
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2013
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The Royal Society of Chemistry
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Kayser, Henning1, Author
Rodríguez-Ropero, Francisco2, Author
Leitner, Walter1, 3, Author           
Fioroni, Marco4, Author
Domínguez de María, Pablo1, Author
Affiliations:
1Institut für Technische und Makromolekulare Chemie (ITMC), RWTH Aachen University, Worringerweg 1, 52074, Aachen, Germany, ou_persistent22              
2Center of Smart Interfaces, Technische Universität Darmstadt, Petersenstraße 32, 64287, Darmstadt, Germany, ou_persistent22              
3Service Department Leitner (Technical Labs), Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_1445626              
4keine Organisation, Konrad Müller Str. 17, 52249, Eschweiler, Germany, ou_persistent22              

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 Abstract: Dicarboxylic acids have been identified as promising catalysts for the depolymerization of cellulose and other polysaccharides. It has been suggested that they might act in “biomimetic” analogy to the active site of glycosidases, where also two carboxylic groups are present, and it is assumed that one residue acts as proton donor and the other one as proton acceptor. In the present paper, a series of structurally distinct carboxylic acids were experimentally assessed as catalysts in the hydrolysis of cellobiose under fully identical acidic conditions. The results clearly show a pH-dependent activity profile in bulk aqueous solutions without any evidence for a cooperative mechanism. In contrast, the protein environment at the active site in glycosidases was found to be essential for the cooperative action of the two carboxylic acid groups. A detailed computational chemistry study is presented, focusing on the protein electric potential, as well as on a reduced dielectric constant (ε) within the active site, resulting from the limited presence of water. These two aspects alter the pKa of the carboxylic acid groups dramatically, providing the necessary local environment for a cooperative proton donor–acceptor mechanism, which cannot be mimicked by simple diacids in bulk aqueous phase.

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Language(s): eng - English
 Dates: 2012-11-162013-03-282013-03-282013-06-28
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1039/C3RA41307A
 Degree: -

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Title: RSC Advances
  Abbreviation : RSC Adv.
Source Genre: Journal
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Publ. Info: Cambridge, UK : Royal Society of Chemistry
Pages: 6 Volume / Issue: 3 (24) Sequence Number: - Start / End Page: 9273 - 9278 Identifier: ISSN: 2046-2069
CoNE: https://pure.mpg.de/cone/journals/resource/2046-2069