Thermal stability of films formed by soy protein isolate–sodium dodecyl sulfate

Schmidt, Vanessa; Giacomelli, Cristiano; Soldi, Valdir

doi:10.1016/j.polymdegradstab.2004.07.003

Cited by 215 publications

(129 citation statements)

References 21 publications

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“…Multiple characteristic absorption bands will be formed in the infrared region, among which the amide _ is located in the 1600∼1700 cm −1 wave band [18], which is led by the stretching vibration of C � O. e wave band ranging from 1615∼1637 cm −1 and 1682∼1700 cm −1 is called β-sheet, 1646∼1664 cm −1 is called α-helix, 1637∼1645 cm −1 is called random coil, and 1664∼1681 cm −1 is called β-turn [19]. As shown in Figure 3, the content of α-helix presented an increased trend from 4°C to −18°C (p < 0.05), while the content of β-sheet and β-turn was quite similar.…”

Section: Secondary Structure Of Myofibrillar Proteins Analysismentioning

confidence: 99%

Effect of Storage Temperatures on the Moisture Migration and Microstructure of Beef

Wang

Mehmood

et al. 2018

Journal of Food Quality

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e e ects of freezing temperature on the microstructure and moisture migration of beef were investigated, aiming to provide the potential theoretical basis for the beef storage. Drip loss, surface hydrophobicity, and secondary structure of myo brillar proteins, ice crystal, and micro-and ultrastructure of meat were analyzed at 4°C, −1°C, −6°C, −9°C, −12°C, and −18°C, respectively. Results indicated that the drip loss and surface hydrophobicity of samples stored at −12°C were signi cantly lower than that stored at 4°C and −1°C (p < 0.05) and no signi cant di erence with −18°C (p > 0.05). Result from Fourier transform infrared spectroscopy suggested that protein denaturation occurred after storage. ere was an increase in α-helices and decline in random coil at lower temperature (−12°C and −18°C). It was indicated that the samples stored at −12°C and −18°C could e ectively restrain the denaturation of protein and maintain the stability of secondary structure. e analysis of the ice crystal and micro-and ultrastructure of the muscle indicated that the structure of samples stored at −12°C and −18°C had more integrity and was complete than that stored at 4°C and −1°C. e spaces (water "reservoir" and "channel") where was the origination of drip were small. Furthermore, the results of low-eld nuclear magnetic resonance and 1 H magnetic relaxation image showed that the freezing at −12°C could inhibit the migration of immobilized water to free water.

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Section: Secondary Structure Of Myofibrillar Proteins Analysismentioning

confidence: 99%

Effect of Storage Temperatures on the Moisture Migration and Microstructure of Beef

Wang

Mehmood

et al. 2018

Journal of Food Quality

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“…Its gaseous products showed absorption bands of CO 2 (2 370, 2 340 and 670 cm (-NH 3 stretching). [13,14] For pure starch, absorptions related to alcohol (O-H stretching at 3 500-3 750 cm À1 ), CO 2, CO and carbonyl compounds 2 360, 2 177 and 1 743 cm À1 , were observed. Starch presented a single degradation step, which reflects weaker link scissions, such as that of C-O bonds.…”

mentioning

confidence: 98%

“…However, at 600 8C smaller amount of solid residue was observed because of the presence of more stable bonds which could not be broken even at this temperature. [13] In a recent work, Schmidt et al [14] studied the thermal stability of SDScontaining soy protein isolate cast films by thermogravimetric analysis (TGA) and infrared spectroscopy (FTIR) under nitrogen atmosphere. Although the same raw material had been used, the methodology of film preparations was different which may contributed to the few differences on peaks intensities at FTIR spetra for soy protein only.…”

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confidence: 99%

Thermal Stability of Biodegradable Films Based on Soy Protein and Corn Starch

Soares¹,

Scremin²,

Soldi³

2005

Macromolecular Symposia

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Summary: In this paper, films were prepared from soy protein and corn starch in different proportions and thermal stability and kinetic parameters were determined through degradation reactions in an inert atmosphere. Solid residues and decomposition products were identified by infrared spectroscopy. Films from corn starch were less thermally stable than soy protein films. The films containing both components had lower thermal stabilities when compared to those of the pure biopolymers. The mechanism of starch thermal degradation seems to occur in a single step, which can be confirmed by the constant E-values during the thermal degradation reaction. For the pure protein and its mixtures an increase in the activation energy was observed during the reaction. Solid residues for protein at different temperatures showed mainly bands related to C O stretching, angular deformation of N-H and C-H groups. For starch, absorptions related to free and bound O-H, C O stretching of CO 2 , CO and carbonyl compounds were observed. For the 50/50 mixture bands related to soy protein and corn starch were observed. The gaseous products for soy protein showed absorptions related to CO 2 , CO, C O, NH 3 and C-H stretching. For pure starch absorptions related to O-H stretching from alcohol, C O from CO 2 , CO and carbonyl compounds. The 50/50 mixture had the same characteristics as pure soy protein and corn starch.

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“…The broad absorbance band observed at nearby 3280 cm -1 is attributable to the free and bounded O-H and N-H groups. The characteristic C-H stretching of the CH 2 -and CH 3 -groups of saturated structures generally appears in the range of 2980-2850 cm -1 (Schmidt et al 2005). Therefore, the FTIR spectra of the SPI-only and zein-only films exhibit three adjacent peaks near 2920, 2870, and 2850 cm -1 , while the native and microwave-modified blended films had only two peaks near 2920 and 2870 cm -1 .…”

Section: Resultsmentioning

confidence: 97%

Effect of microwave modification on mechanical properties and structural characteristics of soy protein isolate and zein blended film

Wang¹,

Gao²,

Wang³

et al. 2016

Czech J. Food Sci.

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Wang N., Gao Y.Z., Wang P., Yang S., Xie T.M., Xiao Z.G. (2016): Effect of microwave modification on mechanical properties and structural characteristics of soy protein isolate and zein blended film. Czech J. Food Sci., 34: 180-188.Soy protein isolate (SPI) and zein were blended at different ratios, and native and microwave-modified films were prepared at pH 12 in an ethanol/water (20 : 80) mixture. The effect of the microwave modification on the mechanical properties and structural characteristics of the SPI and zein blended films was investigated. The results show that the microwave-modified blended film of 3 : 1 SPI-zein demonstrated the best mechanical properties: the highest breaking strength (2900 g) and the highest fracturing distance (16.08 mm). The morphology of the microwave-modified film was more homogeneous and had fewer pinholes than the zein-only film. In addition, the glass transition temperature of the microwave-modified film rose by nearly half compared to the zein-only film, while the melting temperature increased by almost 2.5%. The secondary structure analysis indicates that a moderate amount of microwave treatment will promote a decrease in α-helix, β-turn, and random coil content and an increase in β-sheet content. This study provides an edible material with better flexibility for food packaging.

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Thermal stability of films formed by soy protein isolate–sodium dodecyl sulfate

Cited by 215 publications

References 21 publications

Effect of Storage Temperatures on the Moisture Migration and Microstructure of Beef

Effect of Storage Temperatures on the Moisture Migration and Microstructure of Beef

Thermal Stability of Biodegradable Films Based on Soy Protein and Corn Starch

Effect of microwave modification on mechanical properties and structural characteristics of soy protein isolate and zein blended film

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