FT-IR spectrometric studies of carbohydrates and proteins
Thomas, Andrew Gardner Adams
MetadataShow full item record
Vibrational spectrometry, specifically infrared spectrometry, has been utilized as an analytical method for the interrogation of complex biological systems. Fourier transform infrared (FT-IR) spectrometry yields structurally-specific information that has been applied for both quantitative and qualitative studies. Combination of FT-IR spectrometry with complementary techniques and analytical methods makes it an even more powerful and sensitive tool. Methodologies for the study of glycosidic linkages and structures in glucan carbohydrates have been developed with the use of FT-IR spectrometry, attenuated total reflection (ATR), and chemometrics. Initially, the ability of infrared spectrometry to distinguish different types of linkages was demonstrated through calibration. Further, specific linkage patterns on individual monosaccharide units within carbohydrate chains have been predicted. These methodologies are part of an ongoing effort to predict monosaccharide and linkage information of N-linked mammalian oligosaccharides. The changes in the secondary structure of the dairy protein â -lactoglobulin have been observed and interpreted through FT-IR spectrometry as the protein adsorbed at the oil-water interface of an emulsion system. The protein was competitively displaced from the interface by a small molecule surfactant, and the structural effects were studied. Experiments were also performed to predict the degree of methylesterification of pectins. Calibration models were built that contained both pectin standards and experimentally de-esterified samples.