The method of integrated kinetics and its applicability to the exo-glycosidase-catalyzed hydrolyses of p-nitrophenyl glycosides. Borisova, A., Reddy, S., Ivanen, D., Bobrov, K., Eneyskaya, E., Rychkov, G., Sandgren, M., Stålbrand, H., Sinnott, M., Kulminskaya, A., & Shabalin, K. Carbohydrate Research, 412:43-49, 2015. cited By 2
Paper doi abstract bibtex 1 download In the present work we suggest an efficient method, using the whole time course of the reaction, whereby parameters kcat, Km and product KI for the hydrolysis of a p-nitrophenyl glycoside by an exo-acting glycoside hydrolase can be estimated in a single experiment. Its applicability was demonstrated for three retaining exo-glycoside hydrolases, β-xylosidase from Aspergillus awamori, β-galactosidase from Penicillium sp. and α-galactosidase from Thermotoga maritima (TmGalA). During the analysis of the reaction course catalyzed by the TmGalA enzyme we had observed that a non-enzymatic process, mutarotation of the liberated α-d-galactose, affected the reaction significantly. © 2015 Elsevier Ltd. All rights reserved.
@ARTICLE{Borisova201543,
author={Borisova, A.S. and Reddy, S.K. and Ivanen, D.R. and Bobrov, K.S. and Eneyskaya, E.V. and Rychkov, G.N. and Sandgren, M. and Stålbrand, H. and Sinnott, M.L. and Kulminskaya, A.A. and Shabalin, K.A.},
title={The method of integrated kinetics and its applicability to the exo-glycosidase-catalyzed hydrolyses of p-nitrophenyl glycosides},
journal={Carbohydrate Research},
year={2015},
volume={412},
pages={43-49},
doi={10.1016/j.carres.2015.03.021},
note={cited By 2},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84929649802&doi=10.1016%2fj.carres.2015.03.021&partnerID=40&md5=f216c9f632b9a6d57c20a434a9dbc525},
affiliation={National Research Center Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Orlova roscha, 188300, Russian Federation; Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, Uppsala, Sweden; Department of Biochemistry and Structural Biology, Lund University, Lund, S-221 00, Sweden; Department of Chemical Sciences, University of Huddersfield, Queensgate, Huddersfield, HD1 3DH, United Kingdom; St. Petersburg State Polytechnical University, 29 Politekhnicheskaya st., St. Petersburg, 195251, Russian Federation},
abstract={In the present work we suggest an efficient method, using the whole time course of the reaction, whereby parameters k<inf>cat</inf>, K<inf>m</inf> and product K<inf>I</inf> for the hydrolysis of a p-nitrophenyl glycoside by an exo-acting glycoside hydrolase can be estimated in a single experiment. Its applicability was demonstrated for three retaining exo-glycoside hydrolases, β-xylosidase from Aspergillus awamori, β-galactosidase from Penicillium sp. and α-galactosidase from Thermotoga maritima (TmGalA). During the analysis of the reaction course catalyzed by the TmGalA enzyme we had observed that a non-enzymatic process, mutarotation of the liberated α-d-galactose, affected the reaction significantly. © 2015 Elsevier Ltd. All rights reserved.},
author_keywords={Integrated kinetics; Mutarotation; Retaining glycoside hydrolase},
funding_details={Российский Фонд Фундаментальных Исследований (РФФИ)12-08-00813-a},
}
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