A solid-state NMR study of the immobilization of alpha-chymotrypsin on mesoporous silica
Faure, N. E. and Halling, P. J. and Wimperis, S. (2014) A solid-state NMR study of the immobilization of alpha-chymotrypsin on mesoporous silica. Journal of Physical Chemistry C, 118 (2). pp. 1042-1048. (https://doi.org/10.1021/jp4098414)
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Solid-state NMR spectroscopy was used to characterize a model biocatalyst system consisting of the enzyme α-chymotrypsin covalently immobilized on epoxide-silica ((glycidoxypropyl)trimethoxysilane, GOPS, grafted onto the surface of a silica gel). One- and two-dimensional 1H, 13C, and 29Si magic angle spinning (MAS) NMR techniques were employed. The support system (epoxide-silica) was characterized first and it was possible to assign silicon and carbon species in both the silica and the GOPS linker. After attachment of the protein, carbonyl carbons (175 ppm) in the immobilized enzyme were visible in 13C MAS NMR spectra recorded at B0 = 20 T. A number of further changes were observed in the 13C and 29Si MAS NMR spectra during the immobilization process, arising from a cross-linking of the surface silica species and an opening of the epoxide functional group by nucleophilic attack. This study shows the potential of multinuclear solid-state NMR for obtaining a better understanding of solid biocatalyst systems at the molecular level.
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Item type: Article ID code: 48441 Dates: DateEvent16 January 2014Published20 December 2013Published OnlineNotes: This document is the unedited Author’s version of a Submitted Work that was subsequently accepted for publication in Journal of Physical Chemistry C, copyright © American Chemical Society after peer review. To access the final edited and published work see http://pubs.acs.org/doi/abs/10.1021/jp4098414. Subjects: Science > Chemistry Department: Faculty of Science > Pure and Applied Chemistry Depositing user: Pure Administrator Date deposited: 05 Jun 2014 12:59 Last modified: 08 Apr 2024 21:33 Related URLs: URI: https://strathprints.strath.ac.uk/id/eprint/48441