[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 (0, 3, 5 and 7 kGy) on the emulsifying properties development of pork myofibrillar protein (MP) and sacroplasmic protein (SP). The results showed that emulsifying activities of SP was significantly impaired by the increasing irradiation dose, while that of MP were only observed to be significantly improved at 3 kGy irradiation (P < .05). The increasing irradiation dose caused the increase of SP carbonyl groups and the decrease of its sulfhydryl groups (P < .05), while 3 kGy irradiation decreased the carbonyl groups of MP and increased ?-potential significantly (P < .05). LF-NMR results revealed that the water hydration in MP structure was dose-dependent. FT-IR data displayed that irradiation caused minor change of SP in the amide I region from 1700 to 1600 cm-1, while >=5 kGy irradiation significantly contributed to the denatured aggregated ?-sheet components of MP.
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...
nmrlearner
Journal club
0
02-03-2018 02:16 PM
[NMR paper] Enhanced Spectral Density Mapping through Combined Multiple-Field Deuterium mCH2D Methyl Spin Relaxation NMR Spectroscopy.
Enhanced Spectral Density Mapping through Combined Multiple-Field Deuterium mCH2D Methyl Spin Relaxation NMR Spectroscopy.
Related Articles Enhanced Spectral Density Mapping through Combined Multiple-Field Deuterium mCH2D Methyl Spin Relaxation NMR Spectroscopy.
Methods. 2017 Dec 27;:
Authors: Hsu A, O'Brien PA, Bhattacharya S, Rance M, Palmer AG
Abstract
Quadrupolar relaxation of 2H (D) nuclear spins is a powerful probe of conformational dynamics in biological macromolecules. Deuterium relaxation rate constants are determined by...
nmrlearner
Journal club
0
01-01-2018 02:17 AM
[NMR paper] Combined 1H-Detected Solid-State NMR Spectroscopy and Electron Cryotomography to Study Membrane Proteins across Resolutions in Native Environments.
Combined 1H-Detected Solid-State NMR Spectroscopy and Electron Cryotomography to Study Membrane Proteins across Resolutions in Native Environments.
Related Articles Combined 1H-Detected Solid-State NMR Spectroscopy and Electron Cryotomography to Study Membrane Proteins across Resolutions in Native Environments.
Structure. 2017 Dec 06;:
Authors: Baker LA, Sinnige T, Schellenberger P, de Keyzer J, Siebert CA, Driessen AJM, Baldus M, Grünewald K
Abstract
Membrane proteins remain challenging targets for structural biology,...
nmrlearner
Journal club
0
12-19-2017 11:31 AM
Combined 1H-Detected Solid-State NMR Spectroscopy and Electron Cryotomography to Study Membrane Proteins across Resolutions in Native Environments
Combined 1H-Detected Solid-State NMR Spectroscopy and Electron Cryotomography to Study Membrane Proteins across Resolutions in Native Environments
Publication date: Available online 14 December 2017
Source:Structure</br>
Author(s): Lindsay A. Baker, Tessa Sinnige, Pascale Schellenberger, Jeanine de Keyzer, C. Alistair Siebert, Arnold J.M. Driessen, Marc Baldus, Kay Grünewald</br>
Membrane proteins remain challenging targets for structural biology, despite much effort, as their native environment is heterogeneous and complex. Most methods rely on...
nmrlearner
Journal club
0
12-15-2017 09:07 PM
Large dose hyperpolarized water with dissolution-DNP at high magnetic field
From The DNP-NMR Blog:
Large dose hyperpolarized water with dissolution-DNP at high magnetic field
p.p1 {margin: 0.0px 0.0px 0.0px 36.0px; text-indent: -36.0px; font: 12.0px Helvetica}
Lipsĝ, K.W., et al., Large dose hyperpolarized water with dissolution-DNP at high magnetic field. J. Magn. Reson., 2017. 274: p. 65-72.
http://dx.doi.org/10.1016/j.jmr.2016.11.008
nmrlearner
News from NMR blogs
0
02-25-2017 06:21 AM
[NMR paper] An NMR-based metabolomics study of pork from different crossbreeds and relation to sensory perception.
An NMR-based metabolomics study of pork from different crossbreeds and relation to sensory perception.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles An NMR-based metabolomics study of pork from different crossbreeds and relation to sensory perception.
Meat Sci. 2014 Feb;96(2 Pt A):719-28
Authors: Straadt IK, Aaslyng MD, Bertram HC
Abstract
Meat extracts from five different pig crossbreeds including Duroc/Landrace/Yorkshire (DLY),...
nmrlearner
Journal club
0
07-30-2014 10:22 AM
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...