Faure, Nicole E. and Halling, Peter J. and Wimperis, Stephen (2014) A solid-state NMR study of the immobilization of alpha-chymotrypsin on mesoporous silica. The Journal of Physical Chemistry C, 118 (2). pp. 1042-1048. ISSN 1932-7447
Full text not available from this repository.Abstract
Solid-state NMR spectroscopy was used to characterize a model biocatalyst system consisting of the enzyme alpha-chymotrypsin covalently immobilized on epoxide-silica ((glycidoxypropyl)trimethoxysilane, GOPS, grafted onto the surface of a silica gel). One- and two-dimensional H-1, C-13, and Si-29 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 C-13 MAS NMR spectra recorded at B-o = 20 T. A number of further changes were observed in the C-13 and Si-29 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.