Determination of the domain structure of the <scp>7S</scp> and <scp>11S</scp> globulins from soy proteins by XRD and FTIR

Chen, Jun; Chen, Xiangyan; Zhu, Qingjun; Chen, Fengliang; Zhao, Xiaoyan; Ao, Qiang

doi:10.1002/jsfa.5950

Cited by 126 publications

(54 citation statements)

References 24 publications

(70 reference statements)

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“…The difference in the secondary structure was not observed in the bulk CSPw and CSPa samples based on FTIR analysis (He et al, 2013a). However, the difference in the a-helix and b-sheet structures was also observed in the 7S and 11S globulins from soybean proteins based on XRD analysis (Chen et al, 2013). On the other hand, it is noteworthy that the quantitative data of soy protein sample (SPI) we tested were closer to CSPa, rather than total cottonseed protein (CSPI).…”

Section: Xrd Examinationmentioning

confidence: 69%

“…There were two obvious peaks at 2θ of about 9.4 and 20⁰ in the XRD pattern of the four protein samples. These features are typical for soy protein powders, reflecting the α-helix and β-sheet structures of protein molecules, respectively (Chen et al, 2013;Luo et al, 2016;Zhao et al, 2015). The intensity of both peaks was in the order CSPa < CSPI < CSPa, indicating that the two-step fractionation unequally delivered less α-helix and β-sheet protein components into water-soluble fraction than alkali-soluble fraction.…”

Section: Xrd Examinationmentioning

confidence: 90%

“…Therefore, the objective of the present study was to characterize the surface properties of six cottonseed meal products using scanning electron microscopy (SEM), scanning electron microscopy-energy dispersive spectrometer (SEM-EDS), X-ray diffraction (XRD), and X-ray photoelectron spectroscopy (XPS). For comparison, a commercially available soy protein flour was also examined in the same way as relevant information is available for soy protein powders (Chen et al, 2013;Zhao et al, 2015;. Characterization of surface properties would enhance their potential utilization for various agro-based and industrial purposes.s.…”

Section: Introductionmentioning

confidence: 99%

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Surface Characterization of Cottonseed Meal Products by SEM, SEM-EDS, XRD and XPS Analysis

He¹,

Cheng²,

Olanya³

et al. 2017

JMSR

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The utilization of cottonseed meal products as valuable industrial materials needs to be exploited. We have recently produced water-washed cottonseed meal, total cottonseed protein, sequentially extracted water-and alkali-soluble proteins, and two residues after the total and sequential protein extractions at a pilot scale. In this work, the surface characteristics of the six cottonseed meal products were examined by scanning electron microscopy (SEM), scanning electron microscopy-energy dispersive spectrometer (SEM-EDS), X-ray diffraction (XRD), and X-ray photoelectron spectroscopy (XPS). The results showed that the surface properties of the six products differed from those of a commercial soy protein flour examined comparatively in this work. The compact morphology and relative-high N composition were observed in all three protein products, with greater similarity between the total protein and alkali-soluble protein. The surfaces of the two residue products were more porous with polysaccharide features. Washed cottonseed meal possessed the surface features similar to those of the residues. In the meantime, the N-associated functional groups were under-represented in the surfaces of all samples, compared to their bulk composition. Information derived from this work increased the understanding of the surface functional properties of cottonseed meal products, which would benefit their practical utilization.

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Section: Xrd Examinationmentioning

confidence: 69%

Section: Xrd Examinationmentioning

confidence: 90%

Section: Introductionmentioning

confidence: 99%

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Surface Characterization of Cottonseed Meal Products by SEM, SEM-EDS, XRD and XPS Analysis

He¹,

Cheng²,

Olanya³

et al. 2017

JMSR

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“…7, No. 10; each other, and to those of soy proteins (i. e. 7S and 11S globulins) in the literature (Chen et al, 2013). The peaks at 1653, 1532 and 1236 cm -1 were attributed to amide I (C=O stretching), II (CN stretching, NH bending), and III (CN stretching, NH bending) bands of proteins, respectively (Kong & Yu, 2007;Chen et al, 2013).…”

Section: Secondary Structures Of Cottonseed and Soy Protein Isolatesmentioning

confidence: 80%

Effects of Vigorous Blending on Yield and Quality of Protein Isolates Extracted From Cottonseed and Soy Flours

He¹,

Cao²,

Cheng³

et al. 2013

MAS

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Cottonseed protein has shown great potential as a biodegradable and renewable resource for industrial processes such as the manufacture of wood adhesives. To improve the recovery of the protein from cottonseed flour, we tested the effects of vigorous blending on the extraction efficiency and recovery yield of one-and two-step procedures for isolation of cottonseed protein. For comparison, the effects on one-step soy protein isolation were also examined. Our data indicated that vigorous blending improved the protein recovery from cottonseed and soy flour as much as 40-60%, compared to mild agitation in the extraction phase. The improvement was likely due to the enhanced solid (flour)-liquid (extracting solvent) interaction, and the increased extraction temperature of the vigorous blending process. Similarities in the protein content, molecular mass distribution pattern, and secondary structure of each type of protein isolates processed under different blending treatments indicated that quality of the isolates was not altered by vigorous blending. However, dissimilarities in molecular mass distribution patterns and secondary structures were identified between the different types of isolates (i. e. total, water soluble, and alkali soluble cottonseed proteins, and total soy protein). These differences will enable us to explore in future work the correlations between cottonseed protein structures and industrial use characteristics (such as adhesive properties).

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“…[1] In particular, soy protein is a good alternative ingredient due to its high nutritional value [2] and low cost when compared to other sources of protein. [3] This protein has distinct physiological functions, such as the capacity to reduce cholesterol levels and body fat [4] and the property to prevent several types of cancer. [5] The two main fractions of soy protein are glycinin (11S) and β-conglycinin (7S), which represent approximately 70% of the soybean protein.…”

Section: Introductionmentioning

confidence: 99%

Synergistic Functionality of Soybean 7S and 11S Fractions in Oil-in-Water Emulsions: Effect of Protein Heat Treatment

Perrechil

Ramos

Cunha

2015

International Journal of Food Properties

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Oil-in-water emulsions stabilized by different concentrations of two fractions (7S and 11S) of soy protein, with or without heat treatment at 70 or 90°C, were investigated. Emulsions stabilized by 7S showed smaller droplets than those containing 11S. Moreover, emulsions stabilized by heat treated mixtures enriched in 11S produced gel after high pressure homogenization. Emulsions produced from 75% of 7S and 25% of 11S without or with heat treatment at 70°C showed the smallest droplets, indicating a synergistic effect between them. Thus, the combination between 7S and 11S has a great potential to be used as natural emulsifier in food-grade emulsions.

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Determination of the domain structure of the 7S and 11S globulins from soy proteins by XRD and FTIR

Abstract: This study showed the potential of reverse micelles as a protocol for extracting the 7S and 11S globulins for analytical purposes. The results represent a new avenue for determining the structures of the 7S and 11S globulins.

Cited by 126 publications

References 24 publications

Surface Characterization of Cottonseed Meal Products by SEM, SEM-EDS, XRD and XPS Analysis

Surface Characterization of Cottonseed Meal Products by SEM, SEM-EDS, XRD and XPS Analysis

Effects of Vigorous Blending on Yield and Quality of Protein Isolates Extracted From Cottonseed and Soy Flours

Synergistic Functionality of Soybean 7S and 11S Fractions in Oil-in-Water Emulsions: Effect of Protein Heat Treatment

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