Effects of electron beam irradiation pretreatment on the structural and functional properties of okara protein

Zhang, Meng; Feng, Xumei; Liang, Yulin; He, Mingyu; Geng, Mengjie; Huang, Yuyang; Teng, Fei; Li, Yang

doi:10.1016/j.ifset.2022.103049

Cited by 18 publications

(9 citation statements)

References 52 publications

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“…The maximum fluorescence emission wavelength of all CS–PPI nanoparticles is redshifted from 322.0 nm to 325.5 nm for PPI. A slight redshift is sufficient to indicate that the hydrophobic amino acids within the pea protein isolate are exposed to more polar solvents, which in turn indicate the unfolding of the PPI tertiary structure [ 24 , 25 ]. It may be because the combination of positively charged chitosan and negatively charged pea protein isolate through electrostatic attraction induces the unfolding of PPI, exposing the hydrophobic amino acids to a more polar aqueous environment [ 26 ].…”

Section: Resultsmentioning

confidence: 99%

Fabrication and Characterization of Chitosan–Pea Protein Isolate Nanoparticles

Zhang

Dai

et al. 2022

Molecules

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Chitosan (CS) and pea protein isolate (PPI) were used as raw materials to prepare nanoparticles. The structures and functional properties of the nanoparticles with three ratios (1:1, 1:2 1:3, CS:PPI) were evaluated. The particle sizes of chitosan–pea protein isolate (CS–PPI) nanoparticles with the ratios of 1:1, 1:2, and 1:3 were 802.95 ± 71.94, 807.10 ± 86.22, and 767.75 ± 110.10 nm, respectively, and there were no significant differences. Through the analysis of turbidity, endogenous fluorescence spectroscopy and Fourier transform infrared spectroscopy, the interaction between CS and PPI was mainly caused by electrostatic mutual attraction and hydrogen bonding. In terms of interface properties, the contact angles of nanoparticles with the ratio of 1:1, 1:2, and 1:3 were 119.2°, 112.3°, and 107.0°, respectively. The emulsifying activity (EAI) of the nanoparticles was related to the proportion of protein. The nanoparticle with the ratio of 1:1 had the highest potential and the best thermal stability. From the observation of their morphology by transmission electron microscopy, it could be seen that the nanoparticles with a ratio of 1:3 were the closest to spherical. This study provides a theoretical basis for the design of CS–PPI nanoparticles and their applications in promoting emulsion stabilization and the delivery of active substances using emulsions.

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Section: Resultsmentioning

confidence: 99%

Fabrication and Characterization of Chitosan–Pea Protein Isolate Nanoparticles

Zhang

Dai

et al. 2022

Molecules

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“…With reference to the methods of Zhang et al ( 19 ), it is slightly modified. Sizer Nano ZS90 particle size analyzer was used to determine the particle size of SPC.…”

Section: Methodsmentioning

confidence: 99%

“…With reference to the method of Zhang et al ( 19 ), slightly modified. Field emission scanning electron microscope (Hitachi, Japan) was used to observe the surface microstructure of SPC.…”

Section: Methodsmentioning

confidence: 99%

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Effects of high-pressure homogenization on physicochemical and functional properties of enzymatic hydrolyzed soybean protein concentrate

Liang

Guo²,

Zheng³

et al. 2022

Front. Nutr.

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This paper investigates the effect on the physicochemical and functional properties of soybean protein concentrate (SPC) by using Alcalase protease and high-pressure homogenization (HPH) (0, 20, 40, 60, 80, and 100 MPa) for the combined modification. The results showed that the degree of hydrolysis of SPC was 4.1% and the antigen protein was degraded after Alcalase hydrolysis, when the homogenization pressure (HP) was 6 0Mpa, the particle size of the SPC was the smallest, the zate potential absolute value up to 33.45 mV, the secondary structure has the lowest β-sheet content, the highest random coil content, and the highest surface hydrophobicity (H0), the size of protein fragments on the microstructure surface is the smallest, the lowest denaturation temperature (Td) and enthalpy (△H) are 72.59°C and 1.35 J/g, the highest solubility is 80.54%, and the highest water and oil holding capacities are 7.73 g/g and 6.51 g/g, respectively. The best emulsifying activity and emulsifying stability were 43.46 m2/g and 190.35 min, the most even distribution of emulsion droplets. This indicates that the HPH treatment destroys the structure of enzymatic hydrolyzed SPC, changes its physicochemical properties, and improves its functional properties. In this study, SPC was modified by HPH and enzyme combined treatment, in order to improve the functionality and application range of SPC, and provide a theoretical basis for its high-value utilization in the food field.

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“…It has been demonstrated that EBI can modify protein structure and therefore alter the protein functionality. Zhang et al [ 17 ] showed that EBI reduced the content of α-helix and β-sheet in the secondary structure of the okara protein, increased the surface hydrophobicity and solubility, and improved the emulsifying properties of the okara protein. Liu et al [ 18 ] showed that the S-S bond was broken into an SH bond after EBI, and the α-helix was transformed into β-sheet and unfolded due to the cleavage of covalent bonds, which exposed the buried hydrophobic amino acids of egg white protein; then, the antioxidant activity of egg white protein was improved.…”

Section: Introductionmentioning

confidence: 99%

Electron Beam Irradiation Alters the Physicochemical Properties of Chickpea Proteins and the Peptidomic Profile of Its Digest

Zhang,

Kong,

et al. 2023

Molecules

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Irradiation can be used for the preservation of chickpea protein as it can destroy microorganisms, bacteria, virus, or insects that might be present. However, irradiation may provoke oxidative stress, and therefore modify the functionality and nutritional value of chickpea protein. In order to study the effects of irradiation on the physicochemical properties and digestion behaviour of chickpea protein, chickpea protein concentrate (CPC) was treated with electron beam irradiation (EBI) at doses of 5, 10, 15, and 20 kGy. After irradiation, protein solubility first increased at 10 kGy and 15 kGy, and then decreased at the higher dose of 20 kGy. This was supported by SDS-PAGE, where the intensity of major protein bands first increased and then decreased. Increased doses of EBI generally led to greater oxidative modification of proteins in CPC, indicated by reduced sulfhydryls and increased carbonyls. In addition, the protein structure was modified by EBI as shown by Fourier transform infrared spectroscopy analysis, where α-helix generally decreased, and β-sheet increased. Although the protein digestibility was not significantly affected by EBI, the peptidomic analysis of the digests revealed significant differences among CPC irradiated with varying doses. A total of 337 peptides were identified from CPC irradiated with 0 kGy, 10 kGy, and 20 kGy, with 18 overlapping peptides and 60, 29, and 40 peptides specific to the groups of 0, 10, and 20 kGy respectively. Theoretical calculation showed that the distribution of peptide length, hydrophobicity, net charge, and C-terminal residues were affected by irradiation. The 2, 2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activity showed a marginal decrease with an increasing dose of irradiation. In conclusion, EBI led to oxidative modification and structural changes in chickpea protein, which subsequently affected the physicochemical properties of peptides obtained from in-vitro digestion of CPC, despite similar digestibility.

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Effects of electron beam irradiation pretreatment on the structural and functional properties of okara protein

Cited by 18 publications

References 52 publications

Fabrication and Characterization of Chitosan–Pea Protein Isolate Nanoparticles

Fabrication and Characterization of Chitosan–Pea Protein Isolate Nanoparticles

Effects of high-pressure homogenization on physicochemical and functional properties of enzymatic hydrolyzed soybean protein concentrate

Electron Beam Irradiation Alters the Physicochemical Properties of Chickpea Proteins and the Peptidomic Profile of Its Digest

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