Publication date: Available online 8 October 2015 Source:LWT - Food Science and Technology
Author(s): Jun-Hua Shao, Ya-Min Deng, Li Song, A. Batur, Na Jia, Deng-Yong Liu
The use of LF-NMR technique for assessing the influence of meat protein hydration states on the mobility water and fat in meat batters was investigated. Three relaxation components, T22 (50 ms), T2b and T21 (lower than 10 ms) were found in meat group and fat group. The number of relaxation components in meat batters was not affected by water or fat addition, but the major component T22 clearly shifted to longer relaxation time (from 50 ms to 66 ms) with added water and fat. The relaxation time of heated meat emulsions was lowered, indicating that water and fat proton mobility was limited by heating. A new relaxation component T23 (200-300 ms) was observed after heating, which was deemed as attributing to free water and fat in emulsion gel. Besides, the effect of fat on relaxation time T22 of emulsion gel was higher than water. However, water presented higher influence on T23 in emulsion gel compared to fat. LF-NMR has been clearly demonstrated to be feasible to detect changes in the relaxation times of water and fat caused by different meat protein hydration states initially produced by meat batters with different treatments.
[NMR paper] Effects of solvent concentration and composition on protein dynamics: 13C MAS NMR studies of elastin in glycerol-water mixtures.
Effects of solvent concentration and composition on protein dynamics: 13C MAS NMR studies of elastin in glycerol-water mixtures.
Related Articles Effects of solvent concentration and composition on protein dynamics: 13C MAS NMR studies of elastin in glycerol-water mixtures.
Biochim Biophys Acta. 2015 Apr 24;
Authors: Demuth D, Haase N, Malzacher D, Vogel M
Abstract
We use 13C CP MAS NMR to investigate the dependence of elastin dynamics on the concentration and composition of the solvent at various temperatures. For elastin in...
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04-29-2015 03:49 PM
Effects of solvent concentration and composition on protein dynamics: 13C MAS NMR studies of elastin in glycerol-water mixtures
Effects of solvent concentration and composition on protein dynamics: 13C MAS NMR studies of elastin in glycerol-water mixtures
Publication date: Available online 25 April 2015
Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics</br>
Author(s): Dominik Demuth , Nils Haase , Daniel Malzacher , Michael Vogel</br>
We use 13C CP MAS NMR to investigate the dependence of elastin dynamics on the concentration and composition of the solvent at various temperatures. For elastin in pure glycerol, line-shape analysis shows that larger-scale fluctuations of...
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04-26-2015 03:28 AM
Parting water: â??Electric prismâ?? separates water's nuclear spin states - R & D Magazine
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Parting water: â??Electric prismâ?? separates water's nuclear spin states
R & D Magazine
A method known as nuclear magnetic resonance (NMR) spectroscopy reconstructs protein structures from the relative orientation of the nuclear spins of hydrogen and other atoms. â??Para hydrogen has successfully been used to enhance the sensitivity of the ...
Parting water: â??Electric prismâ?? separates water's nuclear spin states - R & D Magazine
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09-09-2014 09:29 AM
Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation
From The DNP-NMR Blog:
Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation
This article was already published in 2009 but unfortunately I missed it.
Pavlova, A., et al., Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation. Phys. Chem. Chem. Phys., 2009. 11(31): p. 6833-6839.
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11-21-2013 01:14 AM
[NMR paper] Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.
Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.
Related Articles Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.
Biophys J. 2002 Feb;82(2):1086-95
Authors: Perry A, Stypa MP, Tenn BK, Kumashiro KK
Elastin is the principal protein component of the elastic fiber in vertebrate tissue. The waters of hydration in the elastic fiber are believed to play a critical role in the structure and function of this largely hydrophobic, amorphous protein. (13)C CPMAS NMR spectra are acquired for...
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11-24-2010 08:49 PM
[NMR paper] Protein hydration and location of water molecules in oxidized horse heart cytochrome
Protein hydration and location of water molecules in oxidized horse heart cytochrome c by (1)H NMR.
Related Articles Protein hydration and location of water molecules in oxidized horse heart cytochrome c by (1)H NMR.
J Magn Reson. 2000 Nov;147(1):1-8
Authors: Bertini I, Huber JG, Luchinat C, Piccioli M
The hydration properties of the oxidized form of horse heart cytochrome c have been studied by (1)H NMR spectroscopy. Two-dimensional, homonuclear ePHOGSY-NOESY experiments are used to map water-protein interactions. The detected NOEs reveal...
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11-19-2010 08:29 PM
[NMR paper] Stability of beta-galactosidase, a model protein drug, is related to water mobility a
Stability of beta-galactosidase, a model protein drug, is related to water mobility as measured by 17O nuclear magnetic resonance (NMR).
Related Articles Stability of beta-galactosidase, a model protein drug, is related to water mobility as measured by 17O nuclear magnetic resonance (NMR).
Pharm Res. 1993 Jan;10(1):103-8
Authors: Yoshioka S, Aso Y, Izutsu K, Terao T
The inactivation of freeze-dried beta-galactosidase during storage was studied, focusing on the effect of water mobility as measured by the spin-lattice relaxation time, T1, of...
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08-21-2010 11:53 PM
[NMR paper] Structural effects of hydration: studies of lysozyme by 13C solids NMR.
Structural effects of hydration: studies of lysozyme by 13C solids NMR.
Related Articles Structural effects of hydration: studies of lysozyme by 13C solids NMR.
Biopolymers. 1990 Dec;29(14):1801-6
Authors: Kennedy SD, Bryant RG
13C-nmr spectra of lysozyme obtained at 50.3 MHz using both static and magic-angle-spinning-cross-polarization methods are reported at several water contents. The line widths and consequent resolution in the hydrated material is substantially improved over that in the lyophilized protein. The line narrowing is not...
Investigation the effects of protein hydration states on the mobility water and fat in meat batters by LF-NMR technique
Linear Mode
