Infrared Spectroscopy

McKelvy, Marianne L.; Britt, Thomas R.; Davis, Bradley L.; Gillie, J. Kevin; Lentz, L. Alice; Leugers, Anne; Nyquist, Richard A.; Putzig, C. L.

doi:10.1021/a1960003c

Cited by 63 publications

(26 citation statements)

References 876 publications

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“…Fluorescence spectroscopy is another analytical tool for studying proteins, but this method is unable to determine the peptide backbone structure and is also limited to the study of the environments of tyrosine and tryptophan side chains (Szöllösi et al, 1987). Nuclear magnetic resonance methods mainly give as detailed and specific information about peptides and proteins in solution and are limited to low molecular weight proteins (McKelvy et al, 1996;Scotter, 1997;Pelton and McLean, 2000). Infrared spectroscopy is another method to study the conformational structure of proteins and polypeptides, but while infrared (NIR) spectroscopy show low spectra resolution for proteins mid-IR spectroscopy presents problems arising from the very strong infrared absorption of water.…”

Section: Introductionmentioning

confidence: 99%

“…Infrared spectroscopy is another method to study the conformational structure of proteins and polypeptides, but while infrared (NIR) spectroscopy show low spectra resolution for proteins mid-IR spectroscopy presents problems arising from the very strong infrared absorption of water. An alternative can be used FT-IR with the introduction of the attenuated total reflection (ATR) technology but the major obstacle of this technique is the need for sophisticated optical materials (Arrondo et al, 1993;McKelvy et al, 1996;Pelton and McLean, 2000). By contrast, Raman spectroscopy is a more suitable and direct technique that overcomes most of the above objections and can be used for solid samples and aqueous solutions, providing information on the peptide backbone structure, the environment of some side chains such as those of tyrosine and tryptophan (hydrophobic groups), and the local conformations of disulphide bonds and methionine residues (Frushour and Koening, 1975a;Tu, 1982;Pelton and McLean, 2000;Tuma, 2005).…”

Section: Introductionmentioning

confidence: 99%

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Raman Spectroscopy for Monitoring Protein Structure in Muscle Food Systems

Herrero

2008

Critical Reviews in Food Science and Nutrition

280

266

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Raman spectroscopy offers structural information about complex solid systems such as muscle food proteins. This spectroscopic technique is a powerful and a non-invasive method for the study of protein changes in secondary structure, mainly quantified, analysing the amide I (1650-1680 cm(- 1)) and amide III (1200-1300 cm(- 1)) regions and C-C stretching band (940 cm(- 1)), as well as modifications in protein local environments (tryptophan residues, tyrosil doublet, aliphatic aminoacids bands) of muscle food systems. Raman spectroscopy has been used to determine structural changes in isolated myofibrillar and connective tissue proteins by the addition of different compounds and by the effect of the conservation process such as freezing and frozen storage. It has been also shown that Raman spectroscopy is particularly useful for monitoring in situ protein structural changes in muscle food during frozen storage. Besides, the possibilities of using protein structural changes of intact muscle to predict the protein functional properties and the sensory attributes of muscle foods have been also investigated. In addition, the application of Raman spectroscopy to study changes in the protein structure during the elaboration of muscle food products has been demonstrated.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Raman Spectroscopy for Monitoring Protein Structure in Muscle Food Systems

Herrero

2008

Critical Reviews in Food Science and Nutrition

280

266

View full text Add to dashboard Cite

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“…These molecular bonds, in turn, correspond with different macro‐ and micronutrients. McKelvy et al [], Coates [], and Pasquini [] provide detailed discussions of infrared reflectance spectroscopy theory, practice, and applications. Foley et al [] recognized IR spectroscopy's vast potential for ecological studies, allowing rapid analysis of large quantities of samples to assess intraspecific variability in plant and animal tissues.…”

Section: Introductionmentioning

confidence: 99%

Quantifying soluble carbohydrates in tropical leaves using a portable mid‐infrared sensor: Implications for primate feeding ecology

Dunham

Kane

Rodríguez-Saona

2016

American J Primatol

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Identifying the nutritional composition of food items has significant ramifications for primate feeding ecology, which, in turn, influences investigations of primate sociality, cognition, and conservation. The aim of our study was to analyze water soluble carbohydrate (WSC) concentrations in the leaves of trees common to the Diani Forest of Kenya. Many of these leaves are consumed by black and white colobus monkeys (Colobus angolensis palliatus). We assessed whether the infrared spectral data collected using a portable spectrometer can be used to accurately predict WSC concentrations. WSC content was first quantified using the phenol-sulfuric acid method for young and mature leaves of 24 species and ranged from 1.15% to 9.16% dry weight. Spectral data were recorded with a spectrometer equipped with an attenuated total reflectance accessory (Agilent Cary 630) and analyzed using partial least squares regression. The spectral region from 1600 cm(-1) to 1000 cm(-1) gave unique polysaccharide bands associated with carboxyl, acetyl, and glycosidic linkages of sugar residues. The multivariate analysis gave excellent performance parameters with correlation coefficient (r(2) ) of 0.95 and standard error of cross-validation of 0.6% WSC. We found that IR spectroscopy provides a rapid and accurate technique for analyzing WSC concentrations and offers primatologists many advantages over wet chemistry methods for analyzing nutritional composition. Am. J. Primatol. 78:701-706, 2016. © 2016 Wiley Periodicals, Inc.

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“…Advances in Fourier transform infrared (FT‐IR) spectroscopic instrumentation combined with multivariate data analysis have made this technology ideal for large volume, rapid screening and identification of various analytes. Infrared spectroscopy provides valuable information of the biochemical composition of the samples, especially in the fingerprint region, which have been used for numerous food applications related to quality control and safety (Griffiths and De Haseth 1986; McKelvy and others 1996; Wilson and Tapp 1999). …”

Section: Introductionmentioning

confidence: 99%

Rapid Determination of Sugar Level in Snack Products Using Infrared Spectroscopy

Wang¹,

Rodríguez-Saona²

2012

Journal of Food Science

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The U.S. snack food industry generates billions of dollars in revenue each year and vibrational spectroscopic methods combined with pattern recognition analysis could permit optimization of production rate, quality, and safety of many food products. This research showed that infrared spectroscopy is a powerful technique for near real-time (approximately 1 min) assessment of sugar content in various cereal products.

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Infrared Spectroscopy

Cited by 63 publications

References 876 publications

Raman Spectroscopy for Monitoring Protein Structure in Muscle Food Systems

Raman Spectroscopy for Monitoring Protein Structure in Muscle Food Systems

Quantifying soluble carbohydrates in tropical leaves using a portable mid‐infrared sensor: Implications for primate feeding ecology

Rapid Determination of Sugar Level in Snack Products Using Infrared Spectroscopy

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