Simultaneous measurement of glucose and glutamine in aqueous solutions by near infrared spectroscopy

1995 ◽  
Vol 50 (2) ◽  
pp. 109-125 ◽  
Author(s):  
Hoeil Chung ◽  
Mark A. Arnold ◽  
Martin Rhiel ◽  
David W. Murhammer
Keyword(s):  
Infrared Spectroscopy ◽  
Aqueous Solutions ◽  
Near Infrared Spectroscopy ◽  
Simultaneous Measurement ◽  
Near Infrared

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.

Detection of Hydrate Forms of Lithium and Sodium Perchlorates in Aqueous Solutions Using near Infrared Spectroscopy

2014 ◽  
Vol 22 (2) ◽  
pp. 121-128 ◽  
Author(s):  
Anna G. Davidian ◽  
Andrei G. Kudrev ◽  
Lyubov A. Myund ◽  
Maria K. Khripun
Keyword(s):  
Infrared Spectroscopy ◽  
Aqueous Solutions ◽  
Near Infrared Spectroscopy ◽  
Near Infrared
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