Proteins near-infrared spectroscopy

Infrared spectra of fats and oils are similar regardless of their composition. The principal absorption seen is the carbonyl stretching peak which is virtually identical for all triglyceride oils. The most common appHcation of infrared spectroscopy is the determination of trans fatty acids occurring in a partially hydrogenated fat (58,59). Absorption at 965 - 975 cm is unique to the trans functionaHty. Near infrared spectroscopy has been utilized for simultaneous quantitation of fat, protein, and moisture in grain samples (60). The technique has also been reported to be useful for instmmental determination of iodine value (61). 

Iin, T.P., Hsu, Ch.C Determination of residual moisture in lyophilized protein pharmaceuticals using a rapid and non-invasive method near-infrared spectroscopy. PDA J. Pharm. Sci. Technol. 56, pp. 196-205, 2002... 

R. A. Shaw, S. Kotowich, H. H. Mantsch, and M. Leroux, Quantitation of Protein, Creatinine, and Urea in Urine by Near-Infrared Spectroscopy, Clinical Biochem., 29(1), 11 (1996). 

Fiarthun S, Matischak K, Friedl P. Determination of recombinant protein in animal cell culture supernatant by near-infrared spectroscopy. Anal Biochem 1997,15 Aug 251(l) 73 -78. 

This section on chemical factors related to quality in soybeans is divided into subparts on protein and oil, fatty acids, amino acids, tests for protein, carbohydrates and sugars, and other factors that are often discussed, particularly as soybeans are enhanced for more specific end uses. The other factors include tests for fiber, phosphorus, to-copherols, and isoflavones. The intent is to discuss the importance of these factors, to provide background, and, because of increased use of near-infrared spectroscopy as a measurement method for whole and ground soybeans, to include that technology in the discussion of test measurements. While many primary and other methods for measuring these chemical factors are available, this chapter does not intend to cover those methods. 

Orman, B. A. and Schumann, R. A. Jr. (1991) Comparison of near-infrared spectroscopy calibration methods for the prediction of protein, oil, and starch in maize grain. J. Agric. Food Chem., 39, 883-6. 

Winter, G., 2002a. New methods in monitoring of freeze drying near infrared spectroscopy determination of residue moisture during freeze drying. Proceedings of Protein Stability Confererwe, Breckenridge (CO), USA. 

H. Abe. et al. Non-destructive determination of protein content in a single kernel wheat and soybean by near infrared spectroscopy In Near-Infrared Spectroscopy The Future Waves Proceedings of the Seventh International Conference on Near-Infrared Spectroscopy, A.M.C. Davies, PhU Wifliams co-eds. NIR Publications, Chichester, UK, 1996, p. 457 61. 

R. K. Cho, J. H. Lee, Y. Ozaki, M. Iwamoto. FT-NIR monitoring system for the study of denaturation of proteins at elevated pressures and temperatures. In Leaping ahead with Near Infrared Spectroscopy, Proceedings of the Sixth International Conference on Near-Irfrared Spectroscopy. G. D. Batten, P. C. Flinn, L. A. Welsh, A. B. Blakeney, co-eds. The NIR Spectroscopy Group, Royal Australian Chemical Institute, 1/21 Vale Street, North Melbourne, Australia, 1995, p. 483-486. 

P. C. Williams, S. G. Stevenson, P. M. Starkey, G. C. Hawtin. The application of near infrared spectroscopy to protein testing in pulse breeding programmes. J Sci FoodAgric 29 285-292, 1978. 

M. Manley, L. Van Zyl, B. G. Osborne. Using Fourier transform near infrared spectroscopy in determining kernel hardness, protein and moisture content of whole wheat flour. J Near Infrared Spectrosc 10 71—76, 2002. 

T. Isaksson, B. N. Nilsen. Noninvasive prediction of protein, fat and water in homogenized beef, vacuum packed in plastic bags. Proc. 5th Int. Conf. on Near Infrared Spectroscopy (Haugesund, Norway, 16-20 June 1992). ISBN 0-13-617416-7, 1992, p. 359-364. 

E. Lanza. Determination of moisture, protein, fat, and calories in raw pork and beef by near infrared spectroscopy. 7 Food 5ci 48 471-474,1983. 

T. M. P. Cattaneo, A. Maraboh, S. Barzaghi, R. Giangiacomo. Detection of soy, pea and wheat proteins in milk powder by near infrared spectroscopy. In Near Infrared Spectroscopy Proceedings 10th Intemation Conference, A. M. C. Davies, R. K. Cho, eds. NIR Publications, Chichester, UK, 2002, p. 161-166. 

H. Kamishikiryo, K. Hasegawa, T. Matoba. Stability of 2179 nm as a key wavelength for protein analysis by near-infrared spectroscopy. J Jpn Food Sci Technol 38 850-857, 1991. 

H. Kamishikiryo, Y. Oritani, H. Takamura, T. Matoba. Protein content in milk by near-infrared spectroscopy. J Food Sci 59 313-315,1994. 

A. Purnomoadi, K. K. Batajoo, K. Ueda, F. Terada. Influence of feed source on determination of fat and protein in milk by near-infrared spectroscopy. Int Dairy J 9 447 52, 1999. 

D. Bertrand, P. Robert, D. Lannay, and M. F. Devaux, Application of Principal Component Analysis to the Determination of Fat and Protein Content of Milk by Near Infrared Spectroscopy, Proc. Euro Food Chem. IV, Leon, Norway, 1987, pp. 519-523. 

Various optical detection methods have been used to measure pH in vivo. Fluorescence ratio imaging microscopy using an inverted microscope was used to determine intracellular pH in tumor cells [5], NMR spectroscopy was used to continuously monitor temperature-induced pH changes in fish to study the role of intracellular pH in the maintenance of protein function [27], Additionally, NMR spectroscopy was used to map in-vivo extracellular pH in rat brain gliomas [3], Electron spin resonance (ESR), which is operated at a lower resonance, has been adapted for in-vivo pH measurements because it provides a sufficient RF penetration for deep body organs [28], The non-destructive determination of tissue pH using near-infrared diffuse reflectance spectroscopy (NIRS) has been employed for pH measurements in the muscle during... 

MCD spectroscopy in range 300 to 2000 nm at both ambient and liquid helium (4.2 K) temperatures can yield information about the spin, oxidation, and coordination states of each heme in a multiheme protein such as CCP (75). This technique, in combination with low-temperature X-band EPR spectroscopy, was used to great effect in characterizing the properties of the fully oxidized and MV forms of the P. aeruginosa CCP in solution. At 4.2 K, both hemes in the oxidized enzyme are low-spin ferric, with diagnostic features in the near infrared-MCD (NIR-MCD) spectrum consistent with one heme with His/Met axial coordination and the other with bis-histidine axial coordination this is entirely consistent with the crystal structure. In contrast, at room temperature only the low-potential (bis-histidine coordinated) heme in the C-terminal domain remains completely low-spin, whereas the high-potential (His/Met coordinated) heme exists as mixture of high- and low-spin forms 58). 

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