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

被引：27

作者：

Ravera, Enrico ^{[1
,2
]}

Michaelis, Vladimir K. ^{[3
,4
]}

Ong, Ta-Chung ^{[3
,4
]}

Keeler, Eric G. ^{[3
,4
]}

Martelli, Tommaso ^{[1
,2
]}

Fragai, Marco ^{[1
,2
]}

Griffin, Robert G. ^{[3
,4
]}

Luchinat, Claudio ^{[1
,2
]}

机构：

[1] Univ Florence, Magnet Resonance Ctr CERM, I-50019 Sesto Fiorentino, FI, Italy

[2] Univ Florence, Dept Chem Ugo Schiff, I-50019 Sesto Fiorentino, FI, Italy

[3] MIT, Francis Bitter Magnet Lab, Cambridge, MA 02139 USA

[4] MIT, Dept Chem, Cambridge, MA 02139 USA

来源：

CHEMPHYSCHEM | 2015年 / 16卷 / 13期

基金：

加拿大自然科学与工程研究理事会;

关键词：

biomaterials; biosilica; DNP; enzyme immobilization; solid-state NMR; ANGLE-SPINNING NMR; MAS NMR; RESOLUTION; DIATOMS; C-13;

D O I：

10.1002/cphc.201500549

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Enzymes 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).

引用

页码：2751 / 2754

页数：4

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