2014
DOI: 10.1002/app.41469
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Effects of hydrolysis degree of soy protein isolate on the structure and performance of hydrolyzed soy protein isolate/urea/formaldehyde copolymer resin

Abstract: The hydrolyzed soy protein isolate (HSPI) with different hydrolysis degree was applied to modify urea‐formaldehyde resins (UF) via copolymerization process. The properties of HSPI were characterized by attenuated total reflection Fourier transform infrared spectroscopy (ATR‐FTIR) and TGA. The results show that HSPI with different hydrolysis degree is obtained. 1H NMR and ATR‐FTIR spectra indicate that HSPI with different hydrolysis degree can incorporate into the structure of cured and uncured UF. The UF modif… Show more

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Cited by 38 publications
(29 citation statements)
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References 32 publications
(51 reference statements)
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“…In its native state, the polar groups of the SPI are unavailable because the hydrophobic region of the SPI protein is enclosed by a hydrophilic region, maintained by non-covalent forces and disulfide bonds (Qu et al 2015). The processing conditions applied for the production of SPI emulsion films in this study, namely alkaline conditions (Qu et al 2015), heating (Keerati-u-rai and Corredig 2010), and the homogenization process (Damodaran 2008), can partially or fully denature the proteins and expose their functional groups, cleave disulfide bonds, and expose hydrophobic and sulfhydryl groups. After this process, probably the tertiary and quaternary structures were disrupted, exposing the hydrophobic side chains of the SPI and making them available to bind to VCO and the nonpolar side of the lecithin molecule.…”
Section: Properties Of the Emulsion-based Edible Filmsmentioning
confidence: 99%
“…In its native state, the polar groups of the SPI are unavailable because the hydrophobic region of the SPI protein is enclosed by a hydrophilic region, maintained by non-covalent forces and disulfide bonds (Qu et al 2015). The processing conditions applied for the production of SPI emulsion films in this study, namely alkaline conditions (Qu et al 2015), heating (Keerati-u-rai and Corredig 2010), and the homogenization process (Damodaran 2008), can partially or fully denature the proteins and expose their functional groups, cleave disulfide bonds, and expose hydrophobic and sulfhydryl groups. After this process, probably the tertiary and quaternary structures were disrupted, exposing the hydrophobic side chains of the SPI and making them available to bind to VCO and the nonpolar side of the lecithin molecule.…”
Section: Properties Of the Emulsion-based Edible Filmsmentioning
confidence: 99%
“…Two decomposition stages were observed. Stage one (< 150 °C) reflected the volatilization of adsorbed water and bound water (Qu et al 2015). Stage two (150 to 400 °C) comprised the decomposition of holocellulose.…”
Section: Tga and Dtg Of Uv-treated Rice Strawmentioning
confidence: 99%
“…2a), which caused an increase in the relative concentration of lignin in straw. The enlarged temperature interval of T3 was in relation to the relatively high concentration of lignin (Qu et al 2015).…”
Section: Thermogravimetric Analysismentioning
confidence: 99%