Influence of extraction and solubilizing treatments on the molecular structure and functional properties of peanut protein

Ma, Tiezheng; Zhu, Hongguang; Wang, Jing; Wang, Qiang; Yu, Liangli; Sun, Baoguo

doi:10.1016/j.lwt.2017.01.037

Cited by 35 publications

(27 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…However, it could be seen that the secondary structure of the α-helixes disappeared, and the content of β-turns (1687 cm −1 ) was largely decreased, while random coils (1642 cm −1 ) emerged in the DWMPH ( Figure 5 B). This result was in agreement with the previous research, that the β-turn structure largely disappeared and the content of the irregular structure was increased in the peanut protein hydrolysates [ 31 ]. Furthermore, a loss of α-helixes is considered to be strongly connected with the increased antioxidant activity of peptides [ 32 ].…”

Section: Resultssupporting

confidence: 93%

Walnut Protein Hydrolysates Play a Protective Role on Neurotoxicity Induced by d-Galactose and Aluminum Chloride in Mice

et al. 2018

View full text Add to dashboard Cite

In recent years, with an increase in the aging population, neurodegenerative diseases have attracted more and more attention. This study aimed to investigate the potential neuroprotective effect of defatted walnut meal protein hydrolysates (DWMPH) on neurotoxicity induced by d-galactose (d-gal) and aluminum chloride (AlCl3) in mice. The animal models were established by combining treatments with d-gal (200 mg/kg/day, subcutaneously) and AlCl3 (100 mg/kg in drinking water) for 90 days. During the 90 days, 1 g/kg of DWMPH was administrated orally every day. The results indicated that DWMPH treatment alleviated oxidative stress, reversed cholinergic dysfunction, and suppressed the release of proinflammatory cytokines in the brains of d-gal + AlCl3-treated mice, and thus improving the learning and memory functions of these mice, which was closely correlated with the strong antioxidant activity of DWMPH. This finding suggests that DWMPH might be a promising dietary supplement in improving neuronal dysfunctions of the brain.

show abstract

Section: Resultssupporting

confidence: 93%

Walnut Protein Hydrolysates Play a Protective Role on Neurotoxicity Induced by d-Galactose and Aluminum Chloride in Mice

et al. 2018

View full text Add to dashboard Cite

show abstract

“…Protein can diffuse rapidly and absorb at the oil–water interface with an improvement in solubility. However, the decrease in α ‐helix and increase in β ‐sheet structures induced the aggregation of protein, and reduced the solubility of protein, which had a positive correlation with the emulsifying property of peanut protein 37 . The increase in β ‐sheet structures also contributed to the exposure of hydrophobic regions, which resulted in an increase in surface hydrophobicity corresponding to the fluorescence analysis.…”

Section: Resultsmentioning

confidence: 99%

Effect of ultrasound‐assisted extraction on the structure and emulsifying properties of peanut protein isolate

et al. 2020

View full text Add to dashboard Cite

BACKGROUNDWith an increasing demand for edible protein, research on new extraction methods is attracting more attention. The effects of such methods on functional properties are important. The present study aimed to evaluate the effect of ultrasound‐assisted extraction on the extraction efficiency, structure, and the emulsifying properties of peanut protein isolate (PPI).RESULTSUltrasound‐assisted extraction significantly improved extraction efficiency and shortened the processing time. The nanostructure, molecular weight distribution, and particle size of PPI were altered by ultrasound‐assisted extraction. The emulsifying properties of the PPI from ultrasound‐assisted extraction were significantly improved compared with alkaline extraction. Peanut protein isolate had lower molecular weight fractions, higher levels of hydrophobic amino acids, and the highest fluorescence intensity with ultrasound intensity, temperature, and time of 3.17 W cm−3, 35 °C, and 30 min, respectively. These contributed to the higher emulsifying activity index and emulsifying stability index of the PPI emulsions. The uniform distribution of droplets and smaller particle size of the PPI emulsions was also observed.CONCLUSIONThe results suggested that ultrasound can be used to induce the conformational changes to modify the interfacial association between protein‐oil phases, thereby improving the emulsifying properties of peanut protein. © 2020 Society of Chemical Industry

show abstract

“…On the other hand, CNPI show bigger globules with less irregular shape and some indentations. The flaky structure of glutelin may be due to the strong alkali environment, and the loose and lamellar structure after extraction is similar to the result of other physical and chemical modifications, such as enzymatic hydrolysis [ 28 ], high-pressure homogenization and succinylation [ 29 ], and these microstructure changes may result in the exposure of hydrophobic amino acid residues and the alteration of protein functional properties. The particle size of CNPI was bigger and with surface depressions because the acid treatment process may lead to aggregation and the formation of a more compact structure.…”

Section: Resultsmentioning

confidence: 99%

Molecular and Functional Properties of Protein Fractions and Isolate from Cashew Nut (Anacardium occidentale L.)

et al. 2018

View full text Add to dashboard Cite

Some molecular and functional properties of albumin (83.6% protein), globulin (95.5% protein), glutelin (81.3% protein) as well as protein isolate (80.7% protein) from cashew nut were investigated. These proteins were subjected to molecular (circular dichroism, gel electrophoresis, scanning electron microscopy) and functional (solubility, emulsification, foaming, water/oil holding capacity) tests. Cashew nut proteins represent an abundant nutrient with well-balanced amino acid composition and could meet the requirements recommended by FAO/WHO. SDS-PAGE pattern indicated cashew nut proteins were mainly composed of a polypeptide with molecular weight (MW) of 53 kDa, which presented two bands with MW of 32 and 21 kDa under reducing conditions. The far-UV CD spectra indicated that cashew proteins were rich in β-sheets. The surface hydrophobicity of the protein isolate was higher than that of the protein fractions. In pH 7.0, the solubility of protein fractions was above 70%, which was higher than protein isolate at any pH. Glutelin had the highest water/oil holding capacity and foaming properties. Protein isolate displayed better emulsifying properties than protein fractions. In summary, cashew nut kernel proteins have potential as valuable nutrition sources and could be used effectively in the food industry.

show abstract

Influence of extraction and solubilizing treatments on the molecular structure and functional properties of peanut protein

Cited by 35 publications

References 31 publications

Walnut Protein Hydrolysates Play a Protective Role on Neurotoxicity Induced by d-Galactose and Aluminum Chloride in Mice

Walnut Protein Hydrolysates Play a Protective Role on Neurotoxicity Induced by d-Galactose and Aluminum Chloride in Mice

Effect of ultrasound‐assisted extraction on the structure and emulsifying properties of peanut protein isolate

Molecular and Functional Properties of Protein Fractions and Isolate from Cashew Nut (Anacardium occidentale L.)

Contact Info

Product

Resources

About