1998
DOI: 10.1006/jcis.1998.5751
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FTIR Study of Hydration Phenomena in Protein–Sugar Systems

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Cited by 66 publications
(47 citation statements)
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“…In our previous FTIR study [21], the bands at 1647 cm −1 in the spectra corresponded to the gelatin’s amide I band due to CO stretching. The results showed a red shift in amide I band to the lower wavenumber indicating the hydrogen bonding of the CO in gelatin to the silanol hydrogen [38]. These interactions could be used to induce physical cross-linkage [39, 40].…”
Section: Discussionmentioning
confidence: 99%
“…In our previous FTIR study [21], the bands at 1647 cm −1 in the spectra corresponded to the gelatin’s amide I band due to CO stretching. The results showed a red shift in amide I band to the lower wavenumber indicating the hydrogen bonding of the CO in gelatin to the silanol hydrogen [38]. These interactions could be used to induce physical cross-linkage [39, 40].…”
Section: Discussionmentioning
confidence: 99%
“…These chemical changes would lead to several changes in the mid-IR spectrum (Farhat, Orset, Moreau, & Blanshard, 1998). Fig.…”
Section: Ft-ir Analysis Of Lzm Trg and Lzmetrg Conjugatesmentioning
confidence: 98%
“…FTIR spectroscopy is a particularly useful technique for the study of protein-carbohydrate systems (14), as there are several readily identifiable regions of the midinfrared spectrum where the chemical fingerprints of carbohydrates and proteins do not overlap significantly. The most distinctive spectral features for proteins are the strong amide I and II bands centered at approximately at 1650 and 1540 cm -1 respectively.…”
Section: Resultsmentioning
confidence: 99%