2010
DOI: 10.1016/j.jfoodeng.2010.03.039
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Mechanical and thermal properties of soy protein films processed by casting and compression

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Cited by 179 publications
(95 citation statements)
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“…On the other hand, the band at 1400 cm −1 , corresponding to the vibrations of COO − group, appears due to the amphoteric character of proteins where the carboxyl group could be ionized since the film forming solution was adjusted at alkaline pH. Guerrero et al [14] and Guerrero and De La Caba [43] obtained similar FTIR spectral data for soy protein edible films with glycerol as a plasticizer.…”
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confidence: 81%
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“…On the other hand, the band at 1400 cm −1 , corresponding to the vibrations of COO − group, appears due to the amphoteric character of proteins where the carboxyl group could be ionized since the film forming solution was adjusted at alkaline pH. Guerrero et al [14] and Guerrero and De La Caba [43] obtained similar FTIR spectral data for soy protein edible films with glycerol as a plasticizer.…”
mentioning
confidence: 81%
“…Journal of Food Quality The broad band of 3500-3000 cm −1 is attributable to free and bound OH and NH groups, which are able to form hydrogen bonds with the carbonyl group of the peptides in the proteins [14,43]. Protein concentrates from other studied bean varieties showed the same type of infrared spectra (data not shown).…”
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confidence: 85%
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“…1d) lacks of these peaks. Proteins presented as well a broad band above 3500 cm -1 range, related to free and bound O-H and N-H groups, which are able to form hydrogen bonding with the carbonyl group of the peptide linkage in the protein (Guerero et al, 2010). For carbohydrates, spectroscopic regions from 3550-3200 cm -1 and 3650-3580 cm -1 correspond to O−H stretching (Coimbra et al, 2010) as well.…”
Section: Tensile Strength and Percentage Of Elongationmentioning
confidence: 99%
“…Proteins present a large variety of possible interactions and chemical reactions (Hernández Izquierdo and Krochta 2008); they may participle in chemical reactions through covalent (peptide and disulfide) linkages and noncovalent interactions (ionic hydrogen and van der Waals bonding). In addition, hydrophobic interactions occur between non-polar groups of amino acids chains (Guerrero et al 2010). Interlinkages between proteins participating in the formation of a film can lead to improve film properties.…”
Section: Edible Coatings As a Structural Matrixmentioning
confidence: 99%