Publication date: Available online 9 June 2014 Source:Food Research International
Author(s): Minyi Han , Peng Wang , Xinglian Xu , Guanghong Zhou
The changes of water mobility and fractal dimension (Df) during pork myofibrillar proteins (PMP) heat-induced gelation were investigated using low-field nuclear magnetic resonance (NMR) and image analysis, respectively. The NMR data were related to the gel microstructure which was explained as fractal dimension and pore size using principal component analysis (PCA). Distributed exponential analysis of the T2 relaxation revealed that three water components corresponding to the three water molecule states exist during the heat-induced gelation. A significant change of T2 was occurred when the temperature increased, T21 relaxation times decreased significantly from 403.70ms to 231.01ms with the temperature increasing from 50 to 70°C. The fraction of T21 distributions declined from 99.27% to 77.01% as the temperature increased from 40 to 60°C. Pronounced different gel network structure was observed during the myofibrillar proteins heat-induced gelation and different Df which was determined by box count method was found between all treatments although evidencing a narrow scale range (from 2.835 to 2.860). Good correlations were detected between the NMR T2 parameters and microstructural data. Overall, combined low-field NMR, image analysis and PCA provide powerful tools for elucidating the pork myofibrillar protein heat-induced gelation.
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Abstract
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Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 222</br>
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Modern solid-state NMR methods can acquire high-resolution protein spectra for structure determination. However, these methods use rapid sample spinning and intense decoupling fields that can heat and denature the protein being studied. Here we present a strategy to avoid destroying valuable samples. We advocate first creating a sacrificial sample, which contains unlabeled protein (or no protein) in buffer...
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Heat Management Strategies for Solid-state NMR of Functional Proteins
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Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Daniel J. Fowler, Michael J. Harris, Lynmarie K. Thompson</br>
Modern solid-state NMR methods can acquire high-resolution protein spectra for structure determination. However, these methods use rapid sample spinning and intense decoupling fields that can heat and denature the protein being studied. Here we present a strategy to avoid destroying valuable samples. We advocate first creating a sacrificial sample, which contains unlabeled...
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NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by t
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[NMR paper] NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c i
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Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics
Linear Mode
