Biosilica‐Entrapped Enzymes Studied by Using Dynamic Nuclear‐Polarization‐Enhanced High‐Field NMR Spectroscopy

ChemPhysChem - Tập 16 Số 13 - Trang 2751-2754 - 2015
Enrico Ravera1,2, Vladimir K. Michaelis3,2, Ta‐Chung Ong4,3, Eric G. Keeler3, Tommaso Martelli5,1, Marco Fragai1, Robert G. Griffin6,3,7, Claudio Luchinat6,1,7
1Magnetic Resonance Center (CERM) and Department of Chemistry "Ugo Schiff", University of Florence, 50019 Sesto Fiorentino (FI) (Italy)
2These authors contributed equally
3Francis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
4Current address: Department of Chemistry, Laboratory of Inorganic Chemistry, ETH- Zürich, CH-8093 Zürich (Switzerland)
5Current address: Giotto Biotech Srl, Via Madonna del Piano 6, 50019 Sesto Fiorentino (FI) (Italy)
6Claudio Luchinat, Magnetic Resonance Center (CERM) and Department of Chemistry "Ugo Schiff", University of Florence, 50019 Sesto Fiorentino (FI) (Italy)
7Robert G. Griffin, Francis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 02139 (USA)

Tóm tắt

AbstractEnzymes are used as environmentally friendly catalysts in many industrial applications, and are frequently immobilized in a matrix to improve their chemical stability for long‐term storage and reusability. Recently, it was shown that an atomic‐level description of proteins immobilized in a biosilica matrix can be attained by examining their magic‐angle spinning (MAS) NMR spectra. However, even though MAS NMR is an excellent tool for determining structure, it is severely hampered by sensitivity. In this work we provide the proof of principle that NMR characterization of biosilica‐entrapped enzymes could be assisted by high‐field dynamic nuclear polarization (DNP).

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ChemPhysChem

Tập 16 Số 13

2751-2754

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