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Yufei Hua - One of the best experts on this subject based on the ideXlab platform.
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structural modification of Soy Protein by the lipid peroxidation product acrolein
Lwt - Food Science and Technology, 2010Co-Authors: Yufei HuaAbstract:Acrolein was selected as a representative secondary byproduct of lipid peroxidation to investigate the effect of oxidative modification of reactive aldehyde on Soy Protein structure. Acrolein reacted with histidine, lysine and cysteine residues in Soy Protein to form covalent adducts, leading to Protein carbonylation and degradation of sulfhydryl groups. Circular dichroism spectra showed that Soy Protein modification by acrolein was related to loss of α-helix and increase of β-sheet structure. The decrease in solubility, surface hydrophobicity and intrinsic fluorescence indirectly implied that acrolein induced Soy Protein aggregation, and results obtained by size-exclusion chromatography directly showed that gradual aggregation of Soy Protein was induced by increasing concentration of acrolein. Results of sodium dodecyl sulfate polyacrylamide gel electrophoresis indicated that acrolein caused Soy Protein cross-linking which non-disulphide covalent bonds were involved in the formation of cross-linking, and subunits of β-conglycinin were more vulnerable to acrolein than that of glycinin.
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oxidative modification of Soy Protein by peroxyl radicals
Food Chemistry, 2009Co-Authors: Caimeng Zhang, Xiangzhen Kong, Yufei HuaAbstract:Abstract Oxidative modification of Soy Protein by peroxyl radicals generated in a solution containing 2,2’-azobis (2-amidinopropane) dihydrochloride (AAPH) under aerobic condition was investigated. Incubation of Soy Protein with increasing concentration of AAPH resulted in gradual generation of Protein carbonyl derivatives and loss of Protein sulphydryl groups. Circular dichroism spectra indicated that exposure of Soy Protein to AAPH led to loss of α-helix structure. Effect of oxidation on tertiary structure was demonstrated by surface hydrophobicity and tryptophan fluorescence. Surface hydrophobicity steadily decreased, accompanied by loss and burial of some tryptophan residues, indicating that Soy Protein gradually aggregated. The results of the size exclusion chromatogram (SEC) implied that incubation caused an AAPH-dose-dependent increase of fragmentation and aggregation of oxidised Soy Protein. Sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE) indicated that non-disulphide linkages were involved in aggregate formation, and β-conglycinin was more vulnerable to peroxyl radicals than glycinin.
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structural modification of Soy Protein by the lipid peroxidation product malondialdehyde
Journal of the Science of Food and Agriculture, 2009Co-Authors: Caimeng Zhang, Yufei HuaAbstract:BACKGROUND: Protein oxidation results in covalent modification of structure and deterioration of functional properties of target Protein. Oxidation extent of Soy Protein was affected by the content and type of lipid peroxidation (LPO) products in defatted Soybean flours during storage and processing. Malondialdehyde (MDA) was selected as a secondary byproduct of LPO to investigate the effects of oxidative modification of LPO-derived reactive aldehyde on Soy Protein structure. RESULTS: MDA reacted with e-amino and sulfhydryl groups of Soy Protein, and resulted in an increase in Protein carbonyl groups but a decrease in sulfhydryl/disulfide, free amines and lysine. The decrease in solubility, surface hydrophobicity and intrinsic fluorescence indirectly indicated that MDA induced Soy Protein aggregation, and results of high-performance size-exclusion chromatography directly showed that gradual aggregation of Soy Protein was induced by increasing concentration of MDA. Results of electrophoresis indicated that MDA caused Soy Protein aggregation, and non-disulfide covalent bonds were involved in aggregate formation. CONCLUSION: The results showed that sensitivity of Soy Protein was related to MDA concentration. Soy Protein gradually aggregated with increase of MDA concentration; β-conglycinin was more sensitive to MDA modification than glycinin. Copyright © 2009 Society of Chemical Industry
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effect of ionic strength on the heat induced Soy Protein aggregation and the phase separation of Soy Protein aggregate dextran mixtures
Food Hydrocolloids, 2009Co-Authors: Yunhui Cheng, Yufei Hua, Cheng Yang, Steve W CuiAbstract:Abstract The effects of ionic strength on heat-induced aggregation of Soy Protein and phase separation of different Soy Protein aggregates with dextran were investigated. The increase of ionic strength accelerated Protein aggregation as shown by an increase in turbidity, aggregate fraction and particle size of salt-induced aggregates (SA). Adding salt (NaCl) to the aggregates formed at the ionic strength of zero (non-salt aggregates, non-SA), the increase of aggregate size was also found. Zeta potential results evidenced the charge screening effects of NaCl. The results of phase diagrams indicated that the compatibility of mixtures at higher ionic strength was lower than those at lower ionic strength, and SA was more incompatible with dextran than non-SA. The effects of the increase of aggregate size on the phase separation outweighed the ionic strength, which indicated that the depletion interaction also played an important role in the phase separation of Soy Protein aggregates and dextran. CLSM (Confocal Laser Scanning Microscopy) and rheological observations provided additional information of the microstructures of the mixtures.
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gelling property of Soy Protein gum mixtures
Food Hydrocolloids, 2003Co-Authors: Yufei Hua, Steve W Cui, Qi WangAbstract:Abstract Gelling properties of Soy Protein–gum mixtures were determined by small deformation oscillation measurement and the experimental data were analyzed with blending laws of polymers. Gel strength of Soy Protein–carrageenan mixture was found to follow either upper or lower bounds depending on the concentration of the constituents, suggesting the occurring of phase shift. G ′ of Soy Protein–xanthan mixed gel always followed the upper bound, indicating that Soy Protein was the continuous phase regardless variations of the gum concentration. Combination of Soy Protein with propylene glycol alginate (PGA) produced a mixed gel with high gel strength and stayed above the upper bound at all gum concentrations examined. Covalent bonds between PGA and Soy Protein was suggested to contribute to the rigidity. Storage modulus of the mixture of Soy Protein–locust bean gum (LBG) was below the lower bound at low gum concentrations due to the limited demixing process of LBG. G ′ values of the mixture of Soy Protein and LBG–xanthan followed the lower bound but approached upper bound on reducing Protein concentration, suggesting that the presence of Soy Protein might inhibit LBG–xanthan mixture from forming continuous networks.
Wei-hong Zhong - One of the best experts on this subject based on the ideXlab platform.
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Soy-Protein-Based Nanofabrics for Highly Efficient and Multifunctional Air Filtration
ACS Applied Materials & Interfaces, 2016Co-Authors: Hamid Souzandeh, Kyle S. Johnson, Keshava Bhamidipaty, Yu Wang, Wei-hong ZhongAbstract:Proteins are well-known by their numerous active functional groups along the polypeptide chain. The variety of functional groups of Proteins provides a great potential for Proteins to interact with airborne pollutants with varying surface properties. However, to our knowledge, a successful demonstration of this potential has not been reported before. In this work, Soy Protein, a type of abundant plant Protein, has been employed for the first time to fabricate multifunctional air-filtration materials. To take advantage of the functional groups of Soy Protein for air filtration, the Soy Protein was first well denatured to unfold the polypeptide chains and then fabricated into nanofibers with the help of poly(vinyl alcohol). It was found that the resultant nanofabrics showed high filtration efficiency not only for airborne particulates with a broad range of size but also for various toxic gaseous chemicals (e.g., formaldehyde and carbon monoxide), a capability that has not been realized by conventional air-f...
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Soy-Protein-Based Nanofabrics for Highly Efficient and Multifunctional Air Filtration
2016Co-Authors: Hamid Souzandeh, Kyle S. Johnson, Keshava Bhamidipaty, Yu Wang, Wei-hong ZhongAbstract:Proteins are well-known by their numerous active functional groups along the polypeptide chain. The variety of functional groups of Proteins provides a great potential for Proteins to interact with airborne pollutants with varying surface properties. However, to our knowledge, a successful demonstration of this potential has not been reported before. In this work, Soy Protein, a type of abundant plant Protein, has been employed for the first time to fabricate multifunctional air-filtration materials. To take advantage of the functional groups of Soy Protein for air filtration, the Soy Protein was first well denatured to unfold the polypeptide chains and then fabricated into nanofibers with the help of poly(vinyl alcohol). It was found that the resultant nanofabrics showed high filtration efficiency not only for airborne particulates with a broad range of size but also for various toxic gaseous chemicals (e.g., formaldehyde and carbon monoxide), a capability that has not been realized by conventional air-filtering materials. This study indicates that Protein-based nanofabrics are promising nanomaterials for multifunctional air-filtration applications
Wang Zhang - One of the best experts on this subject based on the ideXlab platform.
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Effect of succinylation on the physicochemical properties of Soy Protein hydrolysate
Food Research International, 2001Co-Authors: Allaoua Achouri, Wang ZhangAbstract:Abstract The combined effect of enzymatic hydrolysis of Soy Protein isolate and the influence of various levels of succinylation on the physicochemical properties of resulting Soy Protein hydrolysate (SPH) have been studied. The results indicated that proteolysis followed by succinylation resulted in a major soluble Protein fraction having a molecular weight of 7 kDa. Depending on the level of modification, succinylation appeared to cause both dissociation of the higher molecular weight fractions (1000 and 400 kDa), and re-association of polypeptides as a result of intermolecular hydrophobic interactions. Surface hydrophobicity (S 0 ) of SPH decreased drastically due to the higher degree of hydrolysis value applied. Additionally, the significant increase in the net charge and elcectrostatic repulsion caused the molecules to expend and undergo conformational changes as reflected by the changes in the hydrophobicity and fluorescence intensity data. Total essential amino acid content was slightly lowered at the highest degree of modification. Low degrees of succinylation improved the in vitro digestibility of the Soy Protein hydrolysates, and the highest value was observed at 69.5% succinylation.
Hamid Souzandeh - One of the best experts on this subject based on the ideXlab platform.
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Soy-Protein-Based Nanofabrics for Highly Efficient and Multifunctional Air Filtration
ACS Applied Materials & Interfaces, 2016Co-Authors: Hamid Souzandeh, Kyle S. Johnson, Keshava Bhamidipaty, Yu Wang, Wei-hong ZhongAbstract:Proteins are well-known by their numerous active functional groups along the polypeptide chain. The variety of functional groups of Proteins provides a great potential for Proteins to interact with airborne pollutants with varying surface properties. However, to our knowledge, a successful demonstration of this potential has not been reported before. In this work, Soy Protein, a type of abundant plant Protein, has been employed for the first time to fabricate multifunctional air-filtration materials. To take advantage of the functional groups of Soy Protein for air filtration, the Soy Protein was first well denatured to unfold the polypeptide chains and then fabricated into nanofibers with the help of poly(vinyl alcohol). It was found that the resultant nanofabrics showed high filtration efficiency not only for airborne particulates with a broad range of size but also for various toxic gaseous chemicals (e.g., formaldehyde and carbon monoxide), a capability that has not been realized by conventional air-f...
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Soy-Protein-Based Nanofabrics for Highly Efficient and Multifunctional Air Filtration
2016Co-Authors: Hamid Souzandeh, Kyle S. Johnson, Keshava Bhamidipaty, Yu Wang, Wei-hong ZhongAbstract:Proteins are well-known by their numerous active functional groups along the polypeptide chain. The variety of functional groups of Proteins provides a great potential for Proteins to interact with airborne pollutants with varying surface properties. However, to our knowledge, a successful demonstration of this potential has not been reported before. In this work, Soy Protein, a type of abundant plant Protein, has been employed for the first time to fabricate multifunctional air-filtration materials. To take advantage of the functional groups of Soy Protein for air filtration, the Soy Protein was first well denatured to unfold the polypeptide chains and then fabricated into nanofibers with the help of poly(vinyl alcohol). It was found that the resultant nanofabrics showed high filtration efficiency not only for airborne particulates with a broad range of size but also for various toxic gaseous chemicals (e.g., formaldehyde and carbon monoxide), a capability that has not been realized by conventional air-filtering materials. This study indicates that Protein-based nanofabrics are promising nanomaterials for multifunctional air-filtration applications
Xiuzhi Susan Sun - One of the best experts on this subject based on the ideXlab platform.
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Adhesion properties of Soy Protein adhesives enhanced by biomass lignin
International Journal of Adhesion and Adhesives, 2017Co-Authors: Sarocha Pradyawong, Xiuzhi Susan SunAbstract:Abstract Soy Protein adhesives have great potential as sustainable eco-friendly adhesives. However, low adhesion under wet conditions hinders its applications. The objective of this research was to enhance the water resistance of Soy Protein adhesives. The focus of this research was to understand the effect of Protein to lignin ratio and lignin particle size i.e. large (35.66 μm), medium (19.13 μm), and small (10.26 μm) on the adhesion performance of Soy Protein adhesives as well as to characterize its rheological and thermal properties. Results showed that the lignin particle size and the Protein to lignin ratio greatly affected the adhesion performance of Soy Protein adhesives. The addition of lignin slightly increased the viscosity, spreadability, and thermostability of Soy Protein adhesives. The wet strength of Soy Protein adhesives increased as lignin particle size decreased. Soy Protein mixed with small size lignin at a Protein to lignin ratio of 10:2 (w/w) at 12% concentration presented the lowest contact angle and the highest wet adhesion strength of 4.66 MPa., which is 53.3% higher than that of 10% pure Soy Protein adhesive. The improvements in adhesion performance and physicochemical properties of Soy Protein adhesives by lignin were ascribed to the interactions between Protein and lignin. Lignin with smaller particle size increased the wet shear strength of Soy Protein adhesives because a larger surface area of lignin was available to interact with the Protein.
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Adhesion and Physicochemical Properties of Soy Protein Modified by Sodium Bisulfite
JAOCS Journal of the American Oil Chemists' Society, 2013Co-Authors: Guangyan Qi, Ningbo Li, Xiuzhi Susan SunAbstract:Soy Protein adhesives with a high solid content (28-39 %) were extracted from Soy flour slurry modified with sodium bisulfite (NaHSO3) at different concentrations. 11S-dominated Soy Protein fractions (SP 5.4) and 7S-dominated Soy Protein fractions (SP 4.5) were precipitated at pH 5.4 and pH 4.5, respectively. The objective of this work was to study the effects of NaHSO3 on adhesion and physicochemical properties of Soy Protein. The adhesion performance of NaHSO3-modified SP 4.5 was better than SP 5.4; the wet strength of these two fractions was from 2.5 to 3.2 MPa compared with 1.6 MPa of control Soy Protein isolate. SDS-PAGE results revealed the reducing effects of NaHSO3 on Soy Protein. The isoelectric pH of Soy Protein decreased as NaHSO3 increased due to the induced extra negative charges (RS-SO3-) on the Protein surface. The rheological properties of Soy Protein adhesives were improved significantly. Unmodified samples SP 5.4 and SP 4.5 had clay-like properties and extremely high viscosity, respectively; with 2-8 g/L NaHSO3 modification, both SP 5.4 and SP 4.5 had a viscous cohesive phase with good flowability. Overall, NaHSO3-modified Soy Protein adhesives in our study have many advantages over the traditional Soy Protein isolate adhesive such as better adhesion performance, higher solid content but with good flowability and longer shelf life. © 2013 AOCS.
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Physicochemical properties of Soy Protein adhesives obtained by in situ sodium bisulfite modification during acid precipitation
JAOCS Journal of the American Oil Chemists' Society, 2012Co-Authors: Guangyan Qi, Ningbo Li, Xiuzhi Susan SunAbstract:Successful industrial applications of Soy Protein adhesives require high adhesion strength and low viscosity at high solid Protein concentration. This study examined the effects of β-conglycinin (7S) and glycinin (11S) ratios on the physicochemical properties of Soy Protein adhesives. Soy Protein adhesives with various 7S/11S ratios were extracted from Soy flour slurry modified with sodium bisulfite using the acid precipitation method, which is based on the different solubilities of 7S and 11S globulins. Seven glycinin-rich Soy Protein fractions and six β-conglycinin-rich Soy Protein fractions were obtained. The external morphology of the samples changed from the viscous cohesive phase to the clay-like phase without cohesiveness. The viscous cohesive samples had good flowability and good water resistance with a wet adhesion strength of 2.0-2.8 MPa. They were stable for up to several months without phase separation at room temperature. Based on the results, we suggest that proper Protein- Protein interaction, hydration capacity (glycinin-rich Soy Protein fractions), and certain ratios of 7S and 11S (β-conglycinin rich Soy Protein fractions) in the Soy Protein sample are crucial to continuous Protein phase formation. Hydrogen bonding, electrostatic forces, and hydrophobic interactions are involved in maintaining the Protein viscous cohesive network, whereas disulfide bonds do not exert significant effects. This study describes a new way to investigate viscous cohesive Soy Protein systems with high solid Protein content, thus alleviating the disadvantages of traditional methods for studying the adhesive properties of Soy Protein isolates, which tend to have poor water resistance, low solid contents, and short storage life. © AOCS 2011.
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Soy Protein adhesive blends with synthetic latex on wood veneer
JAOCS Journal of the American Oil Chemists' Society, 2011Co-Authors: Guangyan Qi, Xiuzhi Susan SunAbstract:Environmental pollution has prompted an\r\ninterest in and a need for bio-based wood adhesives.\r\nModified Soy Protein has shown adhesion properties similar\r\nto those of formaldehyde based adhesives. The objective of\r\nthis research was to investigate the compatibility of a\r\nmodified Soy Protein (MSP) with six commercial synthetic\r\nlatex adhesives (SLAs). Four different blending ratios of\r\nMSP and SLAs were studied. Adhesion; structural change;\r\nand rheological, thermal, and morphological properties of\r\nthe MSP/SLAs blends were characterized. Dry adhesion\r\nstrength of MSP, SLAs and their blends were all similar\r\nwith 100% wood cohesive failure. Water resistance of all\r\nsix SLAs was improved by blending with MSP in terms of\r\nthe wet adhesion strength. The wet adhesion strength of\r\nMSP/PBG (40/60) blends was 6.416 MPa, as compared to\r\n4.66 MPa of pure PBG (press bond glue, urea formaldehyde\r\nbased resin). Viscosity of MSP/SLAs blends was\r\nreduced significantly and reached the lowest value at\r\n40–60% MSP. Infrared spectra, thermal properties, and\r\nmorphological images indicated that chemical reactions\r\noccurred between Soy Protein and PBG molecules. The\r\nMSP provided some functional groups, such as carboxylic\r\n(–COOH), hydroxyl (–OH) and amino groups (–NH2), that\r\ncross-linked with hydroxymethyl groups (–CH2–OH) of\r\nPBG, and also acted as an acidic catalyst for the selfpolymerization\r\nof urea formaldehyde based resin.
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Isoelectric pH of polyamide-epichlorohydrin modified Soy Protein improved water resistance and adhesion properties
Journal of Applied Polymer Science, 2007Co-Authors: Zhikai Zhong, Xiuzhi Susan SunAbstract:Protein macromolecules derived from plants have been considered as alternative resources for various applications, including adhesives, films, rubbers, and biocomposites. Plant Protein polymers are pH sensitive and need to be modified to meet application performance. This study demonstrated interactions between polyamide-epichlorohydrin (PAE) and Soy Protein as affected by pH and temperature. PAE and Soy Protein molecules formed reversible ionic complexes at room temperature at a pH range of 4-9. The complexation interactions acted as physical crosslinking, which stabilized the Soy Protein structure and increased its denatu ration temperature and enthalpy. The viscosity of adhesives derived from the interaction of PAE and Soy Protein was affected significantly by the complexation formation, denaturation, and pH. The complexation interactions improved the adhesion properties of the PAE/modified Soy Protein. pH also played an important role in the adhesion performance, which was attributed to the pH dependence of the Protein conformation and PAE/sov Protein complexation interactions. © 2006 Wiley Periodicals, Inc.
