Influence of atmospheric-pressure cold plasma-induced oxidation on the structure and functional properties of egg white protein

Baek, Ki Ho; Heo, Ye Seul; Yim, Dong Gyun; Lee, Yee Eun; Kang, Taemin; Kim, Hyun‐Jun; Jo, Cheorun

doi:10.1016/j.ifset.2021.102869

Cited by 26 publications

(6 citation statements)

References 42 publications

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“…Surface hydrophobicity is a fundamental physicochemical property of protein, which is decided by protein conformation and, thus, influences functional properties, such as solubility, foaming, and emulsifying capacity (Baek et al., 2021). Hydrophobicity of the protein is influenced by intrinsic factors, such as constitutive amino acids, size, and shape, and by extrinsic factors, such as ionic strength, temperature, pH, and protein concentration (Bakwo Bassogog et al., 2022).…”

Section: Resultsmentioning

confidence: 99%

Difference analysis of the structure and functional properties among coix seed prolamin fractions (α‐, β‐, and γ‐coixin)

Zhou

et al. 2023

Journal of Food Science

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The differences in proteins in structural characteristics are reported to affect their physicochemical and functional properties. In this study, three types of prolamins (γ‐, α‐, and β‐coixin) derived from coix seed separately distributed among fractions 1–3 extracts. They were studied respecting molecular weight, amino acid composition, secondary structure, microstructure, surface hydrophobicity, solubility, water holding capacity, and oil holding capacity. Results showed that the molecular weights of those three fractions were between 10 and 40 kDa. The secondary structure of those fractions was almost the same, mainly based on β‐sheet and irregular structure. The microstructure of α‐ and γ‐coixin presented an irregular shape, whereas β‐coixin presented a regular spherical shape. Those three fractions exhibited species of abundant essential amino acids with the same amino acid composition but different contents. The β‐coixin fraction had the highest content of hydrophobic amino acids (238.39 mg/g) followed by the α‐coixin fraction (235.05 mg/g), whereas the γ‐coixin fraction had the lowest content (33.27 mg/g). The γ‐coixin fraction has the maximum surface hydrophobicity, whereas the β‐coixin fraction has the highest solubility. In addition, the good amphiphilicity of β‐coixin fraction made it possible to be used as a surfactant. The excellent functional properties of the β‐coixin fraction presented in this research would widen the applications of coix seed prolamins. Practical Application The molecular weights of those three fractions were between 10 and 40 kDa. The secondary structure was almost the same, mainly based on β‐sheet and irregular structure. Those three fractions exhibited species of abundant essential amino acids with the same amino acid composition but different contents. The WHC and OHC of β‐coixin were the best, indicating its potential as a surfactant and forming stable lotion.

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Section: Resultsmentioning

confidence: 99%

Difference analysis of the structure and functional properties among coix seed prolamin fractions (α‐, β‐, and γ‐coixin)

Zhou

et al. 2023

Journal of Food Science

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“…Owing to the lower unfolding extent of the native protein structure (RBP extracted from RB stored for 0 d), a strong ultrasonic intensity is required to unfold the protein structure and promote the steric hindrance and electrostatic repulsion between droplets [ 22 ]. Moderate protein oxidation can unfold the structure of the protein, which enhances the steric hindrance and electrostatic repulsion between droplets; therefore, the ultrasonic intensity required for preparing the optimal RBPE is mild [ 23 ]. Excessive protein oxidation might induce protein aggregation, thus reducing the steric hindrance and electrostatic repulsion between droplets [ 18 ].…”

Section: Resultsmentioning

confidence: 99%

Strategy and Mechanism of Rice Bran Protein Emulsion Stability Based on Rancidity-Induced Protein Oxidation: An Ultrasonic Case Study

Zhou

et al. 2022

Foods

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To provide a strategy for improving the stability of rice bran protein emulsion (RBPE), rice bran proteins (RBPs) with different oxidation extents were prepared from fresh rice bran (RB) stored for different times (0, 1, 3, 5, 10 d), and RBPE was prepared with ultrasonic treatment. The ultrasonic conditions were optimized according to the results of the RBPE’s stability (when RB stored for 0, 1, 3, 5, 10 d, the optimal ultrasonic treatment conditions of RBPE were 500 w and 50 min, 400 w and 30 min, 400 w and 30 min, 300 w and 20 min, 500 w and 50 min, respectively). Additionally, the structural characteristics and the flexibility of RBPE interface protein were characterized, and the results showed that compared with native protein and excessive oxidized protein, the unfolded structure content and flexibility of interface protein of RBPE prepared by moderate oxidized protein under optimal ultrasonic intensity was higher. Furthermore, the correlation analysis showed that the RBPE stability was significantly correlated with the structural characteristics and flexibility of the RBPE interface protein (p < 0.05). In summary, ultrasonic treatment affected the interface protein’s structural characteristics and flexibility, improving the stability of RBPE prepared from oxidized RBP.

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“…During the treatment, the intramolecular S-S bond is broken, which results in the release of free active hydrophobic groups. These groups can then polymerize with other protein molecules, converting intermolecular disulfide bonds to intramolecular disulfide bonds and partial protein refolding [50]. Compared to the other three industrial modifications, the increase in the relative content of intermolecular disulfide bonds was smaller in O-SPI.…”

Section: Disulfide Bond Conformational Analysismentioning

confidence: 97%

“…First, gel samples (3 × 3 × 3 mm 3 ) created via the technique above were placed, for at least 1.5 h, in a 2.5% glutaraldehyde 0.1 M phosphate buffer (pH 7.0). Then, after being washed three times with the same buffer for 10 min, the gel samples were dehydrated by being dipped in a series of solutions (50,70,80,90, and 100%) of ethanol for 10 min per solution. Finally, each sample was lyophilized, sputter-coated with gold, and observed at an acceleration voltage of 10 kV and a magnification of 1000.…”

Section: The Whc Of Gelmentioning

confidence: 99%

Impacts of Industrial Modification on the Structure and Gel Features of Soy Protein Isolate and its Composite Gel with Myofibrillar Protein

Wang

et al. 2023

Foods

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Native soy protein isolate (N-SPI) has a low denaturation point and low solubility, limiting its industrial application. The influence of different industrial modification methods (heat (H), alkaline (A), glycosylation (G), and oxidation (O)) on the structure of SPI, the properties of the gel, and the gel properties of soy protein isolate (SPI) in myofibril protein (MP) was evaluated. The study found that four industrial modifications did not influence the subunit composition of SPI. However, the four industrial modifications altered SPI’s secondary structure and disulfide bond conformation content. A-SPI exhibits the highest surface hydrophobicity and I850/830 ratio but the lowest thermal stability. G-SPI exhibits the highest disulfide bond content and the best gel properties. Compared with MP gel, the addition of H-SPI, A-SPI, G-SPI, and O-SPI components significantly improved the properties of the gel. Additionally, MP-ASPI gel exhibits the best properties and microstructure. Overall, the four industrial modification effects may impact SPI’s structure and gel properties in different ways. A-SPI could be a potential functionality-enhanced soy protein ingredient in comminuted meat products. The present study results will provide a theoretical basis for the industrialized production of SPI.

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Influence of atmospheric-pressure cold plasma-induced oxidation on the structure and functional properties of egg white protein

Cited by 26 publications

References 42 publications

Difference analysis of the structure and functional properties among coix seed prolamin fractions (α‐, β‐, and γ‐coixin)

Difference analysis of the structure and functional properties among coix seed prolamin fractions (α‐, β‐, and γ‐coixin)

Strategy and Mechanism of Rice Bran Protein Emulsion Stability Based on Rancidity-Induced Protein Oxidation: An Ultrasonic Case Study

Impacts of Industrial Modification on the Structure and Gel Features of Soy Protein Isolate and its Composite Gel with Myofibrillar Protein

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