FTIR spectra studies on the secondary structures of 7S and 11S globulins from soybean proteins using AOT reverse micellar extraction

Zhao, Xiaoyan; Chen, Fusheng; Xue, Wei; Lee, Lite

doi:10.1016/j.foodhyd.2007.01.019

Cited by 162 publications

(109 citation statements)

References 41 publications

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“…The relative distribution of the secondary structures in all protein samples were β-sheet (40%) > β-turn (33%) > α-helix (14%) > random coil (12%). The distribution pattern is similar to those of secondary structures of soy 7S and 11S proteins in the literature (Zhang & Hua, 2007;Zhao et al, 2008). Even though chemcial modification (Zhang & Hua, 2007) and extracting solvent (Zhao et al, 2008) could alter the secondary structures, data in Table 3 indicated that the mechanical force of vigorous blending did not exert much effects on these protein secondary structures.…”

Section: Secondary Structures Of Cottonseed and Soy Protein Isolatessupporting

confidence: 72%

“…The distribution pattern is similar to those of secondary structures of soy 7S and 11S proteins in the literature (Zhang & Hua, 2007;Zhao et al, 2008). Even though chemcial modification (Zhang & Hua, 2007) and extracting solvent (Zhao et al, 2008) could alter the secondary structures, data in Table 3 indicated that the mechanical force of vigorous blending did not exert much effects on these protein secondary structures. Similar to the qualitative visual observation of FT-IR spectra, differences in the secondary structures between CSPW and other protein isolates was observed, reflected in higher α-helix and lower β-sheet contents of CSPW.…”

Section: Secondary Structures Of Cottonseed and Soy Protein Isolatessupporting

confidence: 72%

“…On the other hand, bands at 35 and 25 kDa were strong in SPI, but weak in CSPI. It was not clear if these differences were due to the different pHs used in protein extraction and/or precipitation, or to the intrinsic differences in composition of the two types of proteins, although a similar molecular mass distribution pattern of SPI was reported previously (Zhao et al, 2008). Anyway, the different molecular mass patterns of these four protein isolates may provide us with an opportunity to test if any adhesive properties of these protein isolates are relevant to the molecular mass.…”

Section: Polypeptide Composition Of Cottonseed and Soy Protein Isolatesmentioning

confidence: 81%

“…, and β-turn structure to 1,660-1,700 cm -1 minus 1670-1680 cm -1 based on the literature (Zhang & Hua, 2007;Zhao et al, 2008).…”

Section: Fourier Transform Infrared Spectroscopy and Protein Secondarmentioning

confidence: 99%

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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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Section: Secondary Structures Of Cottonseed and Soy Protein Isolatessupporting

confidence: 72%

Section: Secondary Structures Of Cottonseed and Soy Protein Isolatessupporting

confidence: 72%

Section: Polypeptide Composition Of Cottonseed and Soy Protein Isolatesmentioning

confidence: 81%

“…, and β-turn structure to 1,660-1,700 cm -1 minus 1670-1680 cm -1 based on the literature (Zhang & Hua, 2007;Zhao et al, 2008).…”

Section: Fourier Transform Infrared Spectroscopy and Protein Secondarmentioning

confidence: 99%

See 2 more Smart Citations

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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“…It is sensitive to changes of the peptide chain structure (Zhao et al 2008). During the research of protein secondary structure, spectral peaks in amide band Ι (1600-1700cm -1 ) were in common used for identification, which, from recently, is a relatively well-developed method.…”

Section: Infrared Spectroscopic Analysismentioning

confidence: 99%

Microwave-assisted phosphorylation of soybean protein isolates and their physicochemical properties

Wang¹,

Chi²

2012

Czech J. Food Sci.

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Wang X.B., Chi Y.J. (2012): Microwave-assisted phosphorylation of soybean protein isolates and their physicochemical properties. Czech J. Food Sci., 30: 99-107.In order to improve the functional properties of soybean protein isolates (SPI), microwave-assisted phosphorylation (MAP) was applied. The result showed that after microwaving at 600 W for 3 min, the phosphorylation level of SPI reached 35.72 mg/g, emulsifying activity and stability were increased 2 times and 1.4 times, respectively, the solubility was increased by 26.0% and the apparent viscosity was decreased by 13.5%. The charge density, content of sulfhydryl groups, and surface hydrophobicity increased significantly. The infra-red spectroscopic analysis indicated PO 4 3-primary and lysine residues for phosphoric acid esterification. The change of amide bond Ι and fluorescence spectrum of variation suggested that the MAP made the secondary and tertiary structures of SPI into a compact conformation. Compared to the regular phosphorylation, the preparation time applied in MAP of SPI was much shorter. These results indicated that MAP can be used as an efficient method to improve the functional properties of SPI.

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Applications of Vibrational Spectroscopy to Study Protein Structural Changes in Muscle and Meat Batter Systems

Herrero

Carmona

Jiménez‐Colmenero

et al. 2001

Handbook of Vibrational Spectroscopy

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Proteins are the most important structural and functional components of muscle and meat batter systems. Vibrational spectroscopy provides information to determine protein structural changes of this food, since these spectroscopic techniques are direct, nondestructive or noninvasive, and require small sample quantities. Raman spectroscopy offers structural information about secondary and tertiary protein structure, and infrared spectroscopy provides information particularly on protein secondary structure. This chapter reviews the applications of these techniques to protein structural studies of muscle and meat batter systems including the effects of various processing treatments and the possibilities of protein structural changes to assess muscle food quality.

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FTIR spectra studies on the secondary structures of 7S and 11S globulins from soybean proteins using AOT reverse micellar extraction

Cited by 162 publications

References 41 publications

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

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

Microwave-assisted phosphorylation of soybean protein isolates and their physicochemical properties

Applications of Vibrational Spectroscopy to Study Protein Structural Changes in Muscle and Meat Batter Systems

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