A solid-state NMR study of the immobilization of α-chymotrypsin on mesoporous silica

Fauré, N. E., Halling, P. J. and Wimperis, S. (2014) A solid-state NMR study of the immobilization of α-chymotrypsin on mesoporous silica. Journal of Physical Chemistry C, 118(2), pp. 1042-1048. (doi: 10.1021/jp4098414)

Abstract

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.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Wimperis, Professor Stephen and Halling, Professor Peter
• Authors: Fauré, N. E., Halling, P. J., and Wimperis, S.
• College/School: College of Science and Engineering > School of Chemistry
• Journal Name: Journal of Physical Chemistry C
• Publisher: American Chemical Society
• ISSN: 1932-7447
• ISSN (Online): 1932-7455