Oxidative modification of soy protein by peroxyl radicals

Wu, Wei; Zhang, Caimeng; Kong, Xiangzhen; Hua, Yufei

doi:10.1016/j.foodchem.2009.02.049

Cited by 138 publications

(122 citation statements)

References 28 publications

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“…Moreover, with the addition of 15% mannitol, sorbitol and xylitol, the fluorescence intensity of SPI decreased from 872 to 757, 712, and 692, respectively. Previous studies indicated that the fluorescence emission maximum shifted to a shorter wavelength and the fluorescence intensity decreased as the environmental hydrophobicity of fluorophore decreased (Kwaambwa & Maikokera 2007;Wu et al 2009). Although the blue shift of the fluorescence emission maximum of SPI added 15% (w/w) polyols is not significant, the simultaneous decrease in fluorescence intensity in our study is an indicative of conformational changes of SPI.…”

Section: Resultsmentioning

confidence: 97%

Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate

Pan¹,

Meng²,

Jiang³

et al. 2017

Czech J. Food Sci.

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Pan M., Meng X., Jiang L., Yu D., Liu T. (2017): Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate. Czech J. Food Sci., 35: 57-66.Effect of polyols (mannitol, sorbitol, and xylitol) at three concentrations (5, 10, and 15% w/w) on the structure of soy protein isolates (SPI) was investigated. Changes in foaming properties of SPI were then examined with the addition of polyols at different concentrations. The interactions between SPI and polyols resulted in a substantial decrease in protein surface hydrophobicity and intrinsic tryptophan fluorescence intensity, along with the covering of tyrosine. Furthermore, circular dichroism (CD) spectroscopy of SPI suggested that a more ordered and compact conformation was induced by polyols. Consequently, these structural changes led to lower foamability of SPI. An increase in the viscosity of SPI suspension seemed to be advantageous for improving the foam stability of SPI.

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Section: Resultsmentioning

confidence: 97%

Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate

Pan¹,

Meng²,

Jiang³

et al. 2017

Czech J. Food Sci.

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“…The protein can be attacked directly by reactive oxygen species or indirectly by reaction with the by-products of lipid peroxidation, resulting in a number of changes in amino acid residue side chains and protein polypeptide backbone (Shacter, 2000). Therefore, conformation of protein under oxidative stress would change, which has also been observed by many former studies (Wu, Wu, & Hua, 2010;Wu, Zhang, Kong, & Hua, 2009;Ye, Liao, Zhao, & Sun, 2013). As protein emulsifying properties are closely related with its structure, protein oxidation would affect its emulsifying properties.…”

Section: Introductionmentioning

confidence: 91%

“…Oxidized PPI was prepared according to the method described by Wu et al (2009). PPI dispersion (25 mg/mL containing 0.5 mg/mL sodium azide, suspended in 10 mM sodium phosphate buffer, pH 7.4) was mixed with a serial concentration of AAPH and then incubated by continuous shaking under air at 37°C in dark for 24 h. The final concentration of AAPH was 0, 0.04, 0.2, 0.5, 1, 3 and 5 mM.…”

Section: Ppi Oxidationmentioning

confidence: 99%

“…Notes: Values in the same column of the same droplet size index followed by different letters (a-e) are significantly different (p < 0.05); values in the same row followed by different letters (x-y, u) are significantly different (p < 0.05). Wu et al (2009Wu et al ( , 2010 reported that protein oxidation would decrease the surface hydrophobicity of soy protein isolate. In general, protein with relative high surface hydrophobicity would have better emulsifying properties.…”

Section: Stability Of Peanut Beveragementioning

confidence: 99%

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Effect of protein oxidation on the stability of peanut beverage

Lin

Liao

Sun

et al. 2014

CyTA - Journal of Food

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Protein oxidation of peanut beverage and their stability during the storage were investigated. To further investigate the relationship between protein oxidation and peanut beverage stability, peanut protein isolate (PPI) was oxidized by peroxyl radicals derived from 2,2ʹ-azobis (2-amidinopropane) dihydrochloride (AAPH), and the emulsion properties stabilized by oxidized PPI were evaluated. During the storage, protein oxidation happened in the peanut beverage, accompanied by deteriorating their stability. Low storage temperature would lighten the oxidation extent and the peanut beverage instability. High roasting pretreatment of peanut kernels before making peanut beverage would enhance the protein oxidation. Emulsion stabilized by oxidized PPI had larger mean droplet size and lower surface charge. Microstructure of PPI stabilizing emulsion showed that emulsions stabilized by PPI of overoxidation underwent severe droplet aggregation during storage. Protein oxidation was an important factor influencing stability during peanut beverage storage.Keywords: peanut beverage; protein oxidation; stability; peanut protein isolate; emulsion El presente estudio investigó la oxidación experimentada por bebidas de cacahuate y la estabilidad de las mismas durante el almacenamiento. Con el objetivo de examinar a fondo la relación existente entre la oxidación proteica y la estabilidad de bebidas de cacahuate, se oxidó el aislado de proteína de cacahuate (PPI) a través de radicales de peroxil derivados de 2,2ʹ-azobis (2-amidinopropano) dicloridrato (AAPH); además, se estudiaron las propiedades de la emulsión estabilizada por PPI oxidado. Se constató que durante el almacenamiento se presentó la oxidación proteica de las bebidas de cacahuate, acompañada del deterioro de su estabilidad. Se concluyó que bajas temperaturas de almacenamiento ayudarían a reducir tanto el grado de oxidación como la inestabilidad de las bebidas de cacahuate y que la oxidación proteica aumentaría si los granos de cacahuate fueran tratados previamente con un tostado a altas temperaturas. Por otra parte, se observó que en la emulsión estabilizada por el PPI oxidado, las gotas presentaron un tamaño promedio más elevado y una carga superficial más baja. La microestructura de la emulsión estabilizadora del PPI demostró que las emulsiones estabilizadas por el PPI de sobre oxidación, desarrollaron una agregación de gotas muy elevada durante el almacenamiento. La oxidación proteica fue uno de los factores importantes que influyeron en el almacenamiento de las bebidas de cacahuate.Palabras claves: bebida de cacahuate; oxidación proteica; estabilidad; aislado de proteína de cacahuate; emulsión

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“…The secondary structure of the protein was analysed using a far-UV circular dichroism spectrum (CDS) (Jasco J-810; Jasco Corp., Tokyo, Japan) according to the modified method of Wu et al (2009). Spectrum conditions: room temperature, J-810 circular dichroism spectrometer in the range of 190-250 nm, scanning speed 100 nm/min, 0.1 nm of the optical path in the sample cell, 100 mdeg/cm of the sensitivity.…”

Section: Sds-page Analysismentioning

confidence: 99%

Physico-chemical and structural properties of four rice bran protein fractions based on the multiple solvent extraction method

Wang

et al. 2015

Czech J. Food Sci.

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Wang Ch., Xu F., Li D., Zhang M. (2015): Physico-chemical and structural properties of four rice bran protein fractions based on the multiple solvent extraction method. Czech J. Food Sci., 33: 283-291.The physicochemical and structural properties of the concentrated rice bran protein (CRBP) and rice bran protein fractions -RBPF (albumin, globulin, prolamin, and glutelin) were investigated on the basis of multiple solvent extraction method. The protein fractions mainly consisted of essential amino acids except for prolamin. The amino acid composition of concentrated protein was superior to soybean protein isolation, such as valine, methionine, leucine, phenylalanine, and histidine, with similar characteristics of solubility, emulsification, and foaming. Based on the difference in amino acid composition, all these five proteins showed relatively high surface hydrophobicity more than 369.3 of prolamin. CRBP and RBPF were composed of different molecular subunits in SDS-PAGE profile. The circular dichroism spectra (CDS) in synergy showed that the primary structures of RBPF were β-protein folding and random coils with various denaturation temperatures in the range of 78.69°C for glutelin and 92.88°C for globulin. The fluorescence spectrometry assays showed that the blue shift occurred at 348 nm for globulin, while the red shift occurred for the concentrated protein, albumin, and globulin at 356.2, 348.6, and 347.0 nm, respectively. Therefore, the research presents the basic characterisation for further application of natural rice bran protein in the food industry.

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Oxidative modification of soy protein by peroxyl radicals

Cited by 138 publications

References 28 publications

Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate

Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate

Effect of protein oxidation on the stability of peanut beverage

Physico-chemical and structural properties of four rice bran protein fractions based on the multiple solvent extraction method

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