Cellulase adsorption and reactivity on a cellulose surface from flow ellipsometry / S. A. Maurer in Industrial & engineering chemistry research, Vol. 51 N° 35 (Septembre 2012)  

Public ISBD [article]  inIndustrial & engineering chemistry research > Vol. 51 N° 35 (Septembre 2012) . - pp. 11389–11400 Titre : Cellulase adsorption and reactivity on a cellulose surface from flow ellipsometry Type de document : texte imprimé Auteurs : S. A. Maurer, Auteur ; C. N. Bedbrook, Auteur ; C. J. Radke, Auteur Année de publication : 2012 Article en page(s) : pp. 11389–11400 Note générale : Industrial chemistry Langues : Anglais (eng) Mots-clés : Adsorption Ellipsometry Résumé : Enzymatic deconstruction of cellulose occurs at the aqueous/cellulose interface. Most assays to explore cellulase activity, however, are performed in bulk solution and, hence, fail to elucidate surface-reaction kinetics. We use flow ellipsometry to quantify the adsorption and surface reactivity of aqueous cellulase on a model cellulose film substrate. The rate of cellulose digestion at the aqueous/solid interface increases with increasing bulk concentration of enzyme, but only up to a plateau corresponding to the maximum adsorption density of cellulase. Kinetic data are analyzed according to a modified Langmuir–Michaelis–Menten framework including both reversible adsorption of cellulase to the cellulose surface and complexation of surface cellulose chains with adsorbed cellulase. At ambient temperature, the molar turnover number is 0.57 ± 0.08 s–1, commensurate with literature values, and the Langmuir adsorption equilibrium constant, characterizing the binding strength of the cellulase, is 0.086 ± 0.026 ppm–1. The rate-determining step in the surface-reaction sequence is complexation of adsorbed cellulase with the solid-cellulose surface. Simultaneous knowledge of sorption and digestion kinetics is necessary to quantify cellulose deconstruction. ISSN : 0888-5885 En ligne : http://pubs.acs.org/doi/abs/10.1021/ie3008538 [article] Cellulase adsorption and reactivity on a cellulose surface from flow ellipsometry [texte imprimé] / S. A. Maurer, Auteur ; C. N. Bedbrook, Auteur ; C. J. Radke, Auteur . - 2012 . - pp. 11389–11400. Industrial chemistry Langues : Anglais (eng) in Industrial & engineering chemistry research > Vol. 51 N° 35 (Septembre 2012) . - pp. 11389–11400 Mots-clés : Adsorption Ellipsometry Résumé : Enzymatic deconstruction of cellulose occurs at the aqueous/cellulose interface. Most assays to explore cellulase activity, however, are performed in bulk solution and, hence, fail to elucidate surface-reaction kinetics. We use flow ellipsometry to quantify the adsorption and surface reactivity of aqueous cellulase on a model cellulose film substrate. The rate of cellulose digestion at the aqueous/solid interface increases with increasing bulk concentration of enzyme, but only up to a plateau corresponding to the maximum adsorption density of cellulase. Kinetic data are analyzed according to a modified Langmuir–Michaelis–Menten framework including both reversible adsorption of cellulase to the cellulose surface and complexation of surface cellulose chains with adsorbed cellulase. At ambient temperature, the molar turnover number is 0.57 ± 0.08 s–1, commensurate with literature values, and the Langmuir adsorption equilibrium constant, characterizing the binding strength of the cellulase, is 0.086 ± 0.026 ppm–1. The rate-determining step in the surface-reaction sequence is complexation of adsorbed cellulase with the solid-cellulose surface. Simultaneous knowledge of sorption and digestion kinetics is necessary to quantify cellulose deconstruction. ISSN : 0888-5885 En ligne : http://pubs.acs.org/doi/abs/10.1021/ie3008538

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