Glucose induced variation of water structure from temperature dependent near infrared spectra

RSC Advances ◽  
2016 ◽  
Vol 6 (107) ◽  
pp. 105729-105736 ◽  
Author(s):  
Xiaoyu Cui ◽  
Wensheng Cai ◽  
Xueguang Shao
Keyword(s):  
Aqueous Solutions ◽  
Infrared Spectra ◽  
Near Infrared ◽  
Water Structure ◽  
Temperature Dependent ◽  
Near Infrared Spectra ◽  
Induced Variation ◽  
Water Species

The different effects of glucose on water species provide evidence to explain the bioprotective function of carbohydrates in aqueous solutions.

Water can be a probe for sensing glucose in aqueous solutions by temperature dependent near infrared spectra

2017 ◽  
Vol 957 ◽  
pp. 47-54 ◽  
Author(s):  
Xiaoyu Cui ◽  
Xiuwei Liu ◽  
Xiaoming Yu ◽  
Wensheng Cai ◽  
Xueguang Shao
Keyword(s):  
Aqueous Solutions ◽  
Infrared Spectra ◽  
Near Infrared ◽  
Temperature Dependent ◽  
Near Infrared Spectra

Multilevel analysis of temperature dependent near-infrared spectra

Talanta ◽  
2015 ◽  
Vol 131 ◽  
pp. 170-174 ◽  
Author(s):  
Ruifeng Shan ◽  
Yue Zhao ◽  
Mengli Fan ◽  
Xiuwei Liu ◽  
Wensheng Cai ◽  
...  
Keyword(s):  
Multilevel Analysis ◽  
Infrared Spectra ◽  
Near Infrared ◽  
Temperature Dependent ◽  
Near Infrared Spectra

Near Infrared Spectra of Water in Aqueous Solutions of Organic Salts. A Solvation Study of Bu4NBr, , and

1971 ◽  
Vol 49 (12) ◽  
pp. 2008-2013 ◽  
Author(s):  
C. Jolicoeur ◽  
Nguyen Dinh The ◽  
A. Cabana
Keyword(s):  
Infrared Spectrum ◽  
Aqueous Solutions ◽  
Infrared Spectra ◽  
Near Infrared ◽  
The Other ◽  
Simple Analysis ◽  
Organic Salts ◽  
Solvent Interactions ◽  
Near Infrared Spectra ◽  
Qualitative Similarity

The near-infrared spectrum of water at various temperatures and in aqueous solutions of Bu4NBr, [Formula: see text], and [Formula: see text] is studied in the region 0.8–1.2 µ. The spectra are recorded differentially with respect to water by varying the cell lengths as to take into account density changes or the volume occupied by the solutes. A simple analysis of these spectra illustrates the qualitative similarity between the effects of the Bu4N+ ion and that of a temperature decrement on the spectrum of water. On the other hand striking differences are observed in the differential spectra obtained with Bu4NBr and the phenyl substituted: salts. Further differences are exhibited in the relative solute-solvent interactions of [Formula: see text] and [Formula: see text].

Temperature-dependent near-infrared spectroscopy for studying the interactions in protein aqueous solutions

NIR news ◽  
2019 ◽  
Vol 30 (5-6) ◽  
pp. 15-17
Author(s):  
Mian Wang ◽  
Xiaoyu Cui ◽  
Wensheng Cai ◽  
Xueguang Shao
Keyword(s):  
Infrared Spectroscopy ◽  
Aqueous Solutions ◽  
Near Infrared Spectroscopy ◽  
Structural Changes ◽  
Near Infrared ◽  
Molten Globule ◽  
Hydration Shell ◽  
Protein S ◽  
Temperature Dependent ◽  
Water Species

Temperature-dependent near-infrared spectroscopy has been developed for studying quantitative and structural analysis, as well as the molecular interactions. Taking the advantage of the temperature effect on hydrogen bonding, the technique has shown its potential in analyzing the interactions in aqueous solutions. In our recent studies, the structural changes in homo-oligopeptides K5 (penta-lysine), D5 (penta-aspartic acid), and protein (ovalbumin) aqueous solutions were studied by temperature-dependent near-infrared spectroscopy. The thermodynamics and their interaction with water were analyzed with the help of the chemometric methods including continuous wavelet transform, independent component analysis, two-dimensional (2D) correlation analysis, and Gaussian fitting. The results show that the oligopeptide in aqueous solution improves the thermal stability of the water species, and K5 has stronger interaction with water than D5. In the gelation of ovalbumin, the change of the water species with two hydrogen bonds (S2) follows the same phases as the protein. S2 maintains the stability of the protein in native and molten globule states, and the weakening of the hydrogen bond in S2 by high temperature results in the destruction of the hydration shell and makes the ovalbumin clusters form a gel structure.

Near infrared spectra of water and aqueous solutions

1964 ◽  
Vol 14 (1-4) ◽  
pp. 268-278 ◽  
Author(s):  
Hideo Yamatera ◽  
Brian Fitzpatrick ◽  
Gilbert Gordon
Keyword(s):  
Aqueous Solutions ◽  
Infrared Spectra ◽  
Near Infrared ◽  
Near Infrared Spectra
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