Effect of Protein Oxidation on the Conformational Properties of Peanut Protein Isolate

Ye, Lin; Liao, Yi Hung; Zhao, Ming; Sun, Weizheng

doi:10.1155/2013/423254

Cited by 25 publications

(26 citation statements)

References 31 publications

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“…Effect of protein oxidation on their emulsifying properties might be governed by their molecular structure and physicochemical characteristics. Oxidative characteristics of the AAPH-pretreated PPI had been reported by our former study (Ye et al, 2013). The investigation noticed that by incubating with increasing AAPH concentration, PPI oxidation extent enhanced, accompanied by a decreasing surface hydrophobicity and formation of soluble aggregates.…”

Section: Emulsifying Characteristics Of Oxidized Ppisupporting

confidence: 63%

“…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%

“…In general, protein with relative high surface hydrophobicity would have better emulsifying properties. Ye et al (2013) found that protein oxidation would induce the peanut protein conformational changes. Therefore, during storage the peanut beverage, instability might be caused by protein oxidation even though rarely studies had reported the relationship between emulsion stability and oxidized protein.…”

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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Section: Emulsifying Characteristics Of Oxidized Ppisupporting

confidence: 63%

Section: Introductionmentioning

confidence: 91%

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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“…While for the Air plasma the Hb or Mb size is approximately the same as control. The increase in size of Hb and Mb is due to protein aggregation, the other groups 49 50 51 also supported this data that protein size increases due to protein aggregation that is the result of protein oxidation. Hence, this further provides an evidence that the oxidation or modification of protein are in control way, for Air plasma treatment as compared to other gases treatment.…”

Section: Resultsmentioning

confidence: 56%

“…While, control oxidation increase the bandwidth of BSA 48 . Recently published work by Ye et al 50 , observed that lower level of oxidation (carbonylation) could generate soluble protein aggregates that having less particle size. Whereas, higher level of oxidation would induce insoluble aggregates of protein, that results in higher molecular size.…”

Section: Discussionmentioning

confidence: 99%

Influence of reactive species on the modification of biomolecules generated from the soft plasma

Attri

Kumar

Park

et al. 2015

Sci Rep

110

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Plasma medicine is an upcoming research area that has attracted the scientists to explore more deeply the utility of plasma. So, apart from the treating biomaterials and tissues with plasma, we have studied the effect of soft plasma with different feeding gases such as Air, N2 and Ar on modification of biomolecules. Hence, in this work we have used the soft plasma on biomolecules such as proteins ((Hemoglobin (Hb) and Myoglobin (Mb)), calf thymus DNA and amino acids. The structural changes or structural modification of proteins and DNA have been studied using circular dichroism (CD), fluorescence spectroscopy, protein oxidation test, gel electrophoresis, UV-vis spectroscopy, dynamic light scattering (DLS) and 1D NMR, while Liquid Chromatograph/Capillary Electrophoresis-Mass Spectrometer (LC/CE-MS) based on qualitative and quantitative bio-analysis have been used to study the modification of amino acids. Further, the thermal analysis of the protein has been studied with differential scanning calorimetry (DSC) and CD. Additionally, we have performed docking studies of H2O2 with Hb and Mb, which reveals that H2O2 molecules preferably attack the amino acids near heme group. We have also shown that N2 gas plasma has strong deformation action on biomolecules and compared to other gases plasma.

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Effect of Peroxyl‐Radicals‐Induced Oxidative Modification in the Physicochemical and Emulsifying Properties of Walnut Protein

Mao

Wang

Sun

et al. 2020

J Americ Oil Chem Soc

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In this paper, the effects of peroxyl radical oxidation on the physicochemical and functional properties of walnut protein were investigated. Walnut protein isolate (WPI) containing 2,2 0 -azobis(2-amidinopropane) dihydrochloride (AAPH) was oxidatively stressed under aerobic conditions in peroxyl radical-generating media. Incubation of walnut protein with increasing concentration of AAPH resulted in gradual carbonyl generation and free sulfhydryl group degradation. The results of surface hydrophobicity implied that oxidation leads to protein aggregation thus decreasing protein solubility in an AAPH concentration-dependent manner (P < 0.05). Emulsifying properties exhibited a significant increase (P < 0.05) at AAPH concentrations up to 0.2 mM and higher AAPH concentrations reduced the emulsifying capacity of WPI. These results indicate that appropriate oxidation is helpful to improve the emulsifying properties of protein, and with an increase of oxidation degree, emulsifying functional will damage.

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Effect of Protein Oxidation on the Conformational Properties of Peanut Protein Isolate

Cited by 25 publications

References 31 publications

Effect of protein oxidation on the stability of peanut beverage

Effect of protein oxidation on the stability of peanut beverage

Influence of reactive species on the modification of biomolecules generated from the soft plasma

Effect of Peroxyl‐Radicals‐Induced Oxidative Modification in the Physicochemical and Emulsifying Properties of Walnut Protein

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