[NMR paper] Low frequency magnetic field plus high pH promote the quality of pork myofibrillar protein gel: A novel study combined with low field NMR and Raman spectroscopy.
Low frequency magnetic field plus high pH promote the quality of pork myofibrillar protein gel: A novel study combined with low field NMR and Raman spectroscopy.
Related ArticlesLow frequency magnetic field plus high pH promote the quality of pork myofibrillar protein gel: A novel study combined with low field NMR and Raman spectroscopy.
Food Chem. 2020 Apr 22;326:126896
Authors: Yang K, Zhou Y, Guo J, Feng X, Wang X, Wang L, Ma J, Sun W
Abstract
This study investigated the combined effects of low frequency magnetic field (LF-MF) (3.8 mT) and pH (5-7) on pork myofibrillar protein (MP) gel quality. With LF-MF applying, the water ratio and migration rate both changed to varying extents. LF-MF modified secondary structure of MP by exposing tryptophan and tyrosine residues to participate in hydrogen bonding with water, as well changing ?-helix and ?-sheet to varying extents; LF-MF also drove molecular rearrangement and crosslinking. LF-MF brought gel larger and more ordered network to trap more water. And the water holding capacity of gels significantly increased by 2.50% and 2.47% when LF-MF involved at appropriate pH (pH 6.5 and 7.0). Collectively, our results support an optimum treatment (pH 6.5 or 7.0 with applying LF-MF) for the improvement in gel quality of pork MP, and the combination of physical and chemical treatments casts a new light into improving product quality during meat processing.
PMID: 32416422 [PubMed - as supplied by publisher]
[NMR paper] Emulsifying properties development of pork myofibrillar and sacroplasmic protein irradiated at different dose: A combined FT-IR spectroscopy and low-field NMR study.
Emulsifying properties development of pork myofibrillar and sacroplasmic protein irradiated at different dose: A combined FT-IR spectroscopy and low-field NMR study.
Emulsifying properties development of pork myofibrillar and sacroplasmic protein irradiated at different dose: A combined FT-IR spectroscopy and low-field NMR study.
Food Chem. 2018 Jun 30;252:108-114
Authors: Li C, Peng A, He L, Ma S, Wu W, Yang H, Sun X, Zeng Q, Jin G, Zhang J, Ma M
Abstract
The present study investigated the effect of different irradiation dose...
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02-27-2018 12:30 PM
Emulsifying properties development of pork myofibrillar and sacroplasmic protein irradiated at different dose: A combined FT-IR spectroscopy and low-field NMR study
Emulsifying properties development of pork myofibrillar and sacroplasmic protein irradiated at different dose: A combined FT-IR spectroscopy and low-field NMR study
Publication date: 30 June 2018
Source:Food Chemistry, Volume 252</br>
Author(s): Chengliang Li, An Peng, Lichao He, Sumin Ma, Wenmin Wu, Haiyan Yang, Xiuxiu Sun, Qi Zeng, Guofeng Jin, Jianhao Zhang, Meihu Ma</br>
The present study investigated the effect of different irradiation dose (0, 3, 5 and 7 kGy) on the emulsifying properties development of pork myofibrillar protein (MP) and...
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02-03-2018 02:16 PM
[NMR paper] High quality NMR structures: a new force field with implicit water and membrane solvation for Xplor-NIH.
High quality NMR structures: a new force field with implicit water and membrane solvation for Xplor-NIH.
High quality NMR structures: a new force field with implicit water and membrane solvation for Xplor-NIH.
J Biomol NMR. 2016 Dec 29;:
Authors: Tian Y, Schwieters CD, Opella SJ, Marassi FM
Abstract
Structure determination of proteins by NMR is unique in its ability to measure restraints, very accurately, in environments and under conditions that closely mimic those encountered in vivo. For example, advances in solid-state NMR...
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12-31-2016 12:18 PM
High quality NMR structures: a new force field with implicit water and membrane solvation for Xplor-NIH
High quality NMR structures: a new force field with implicit water and membrane solvation for Xplor-NIH
Abstract
Structure determination of proteins by NMR is unique in its ability to measure restraints, very accurately, in environments and under conditions that closely mimic those encountered in vivo. For example, advances in solid-state NMR methods enable structure determination of membrane proteins in detergent-free lipid bilayers, and of large soluble proteins prepared by sedimentation, while parallel advances in solution NMR methods and...
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12-29-2016 09:23 PM
High-Resolution Two-Field Nuclear Magnetic Resonance Spectroscopy
From The DNP-NMR Blog:
High-Resolution Two-Field Nuclear Magnetic Resonance Spectroscopy
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Cousin, S.F., et al., High-Resolution Two-Field Nuclear Magnetic Resonance Spectroscopy. Phys. Chem. Chem. Phys., 2016.
http://dx.doi.org/10.1039/C6CP05422F
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12-06-2016 04:10 AM
High-field liquid state NMR hyperpolarization: a combined DNP/NMRD approach
From The DNP-NMR Blog:
High-field liquid state NMR hyperpolarization: a combined DNP/NMRD approach
Neugebauer, P., et al., High-field liquid state NMR hyperpolarization: a combined DNP/NMRD approach. Phys Chem Chem Phys, 2014. 16(35): p. 18781-18787.
http://www.ncbi.nlm.nih.gov/pubmed/25078259
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08-13-2014 07:50 PM
Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics
Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics
Publication date: Available online 9 June 2014
Source:Food Research International</br>
Author(s): Minyi Han , Peng Wang , Xinglian Xu , Guanghong Zhou</br>
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...
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06-10-2014 04:49 PM
High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field
High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field
Abstract Magic-angle spinning (MAS) solid-state NMR (SSNMR) spectroscopy of uniformly-13C,15N labeled protein samples provides insight into atomic-resolution chemistry and structure. Data collection efficiency has advanced remarkably in the last decade; however, the study of larger proteins is still challenged by relatively low resolution in comparison to solution NMR. In this study, we present a systematic analysis of SSNMR protein spectra acquired at 11.7, 17.6 and 21.1 Tesla (1H frequencies of...
Low frequency magnetic field plus high pH promote the quality of pork myofibrillar protein gel: A novel study combined with low field NMR and Raman spectroscopy.
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