Study on condition of ultrasound-assisted thermo-alkali-modified peanut protein embedding curcumin for nanoparticles

Abstract

This study investigated the effects of ultrasoundassisted thermo-alkali modification on the molecular structure of peanut protein. Further, the preparation conditions involved in embedding curcumin by the modified pea protein were also studied. It was found that within the pH range of 7 \ pH \ 11, with an increase in pH, the content of free sulfhydryl group in peanut protein isolate gradually increased from 10.35 ± 0.63 lmol/g (pH = 7) to 18.26 ± 0.93 lmol/g (pH = 10); and the content of disulfide bonds decreased from 44.62 ± 0.48 lmol/g (pH = 7) to 34.26 ± 2.03 lmol/g (pH = 11). In the ultrasonic power range (P \ 300 W), with an increase in power, the content of free mercapto group in peanut protein isolate gradually increased from 12.44 ± 0.73 lmol/g to 19.46 ± 0.24 lmol/g (P = 250 W); and the content of disulfide bonds decreased from 42.29 ± 1.24 lmol/g to 33.28 ± 0.64 lmol/g (P = 300 W). Within the temperature range of 70 °C \ T \ 90 °C, with an increase in temperature, the content of free sulfhydryl group in peanut protein isolate gradually increased from 10.35 ± 0.94 lmol/g (T = 70 °C) to 19.67 ± 0.68 lmol/g (T = 90 °C), and the content of disulfide bonds decreased from 45.02 ± 2.84 lmol/g (T = 70 °C) to 34.26 ± 2.03 lmol/g (T = 90 °C). Response surface test was used to optimize the preparation conditions of nanoparticles from curcumin. The results showed that the optimum parameters of ultrasonic-assisted modification of peanut protein embedding curcumin were pH = 9.8, heating temperature T = 90 °C, ultrasonic power Q = 225 W, and heating time S = 21 min. Under these conditions, the embedding rate of curcumin reached 83.27 ? 1.06%, the ABTS ? scavenging activity generally decreases with time over the 2 days period measured in PPI solution and PPI nanoparticles (PPN), the ABTS ? scavenging activity decreased from 40.8%, 52.2% and 67.3% to 27.1%, 39.0% and 60.5%, respectively. Compared with pure curcumin, the antioxidant activity was increased at presence of PPI.

Effect of lipoxygenase‐induced oxidation on molecular structure and digestive properties of arachin and conarachin

“…When concentration of DOX increased, equilibrium between sulfhydryl group-disulfide bond exchange reactions broke down while disulfide bonds and sulfhydryl groups were largely oxidized to form sulfone or sulfonic acid, thus suggesting a lack of formation of disulfide bonds during oxidation. These findings are similar to those of Li who observed decreases in free sulfhydryl groups, total sulfhydryl content, and disulfide bonds (Li, Shi, et al, 2020).…”

Identification of angiotensin‐converting enzyme inhibitory peptides from peanut meal (Arachis hypogaea Linn) fermented by Lactobacillus pentosus using MALDI‐TOF–MS and LC–MS/MS

“…Peanut meal (Arachis hypogaea Linn), a byproduct from peanut oil extraction, is a rich source of plant protein with protein content exceeding 50%. However, limitations in their oil extraction technologies significantly denature the protein in peanut meal, thus restricting its application in food processing (Hu et al, 2019;Li et al, 2020).…”

“…Peanut meal ( Arachis hypogaea Linn), a byproduct from peanut oil extraction, is a rich source of plant protein with protein content exceeding 50%. However, limitations in their oil extraction technologies significantly denature the protein in peanut meal, thus restricting its application in food processing (Hu et al., 2019; Li et al., 2020). Studies have shown that microbial fermentation can influence the protein molecular structure, and various microbes can produce different enzyme systems and functional factors (Hu et al., 2023; Zambrano‐Cervantes et al., 2023).…”

Valorization of food industrial waste into protein amyloid fibrils for water and energy applications

“…Pickering emulsions with good thermal and pH stability [74][75][76][77], and films made or blended with peanut proteins displayed potential alternatives to petroleum-based films [78][79][80][81]. Protein hydrolysates prepared using enzymatic hydrolysis showed antioxidative, angiotensin-converting enzyme (ACE) inhibiting activity, and antithrombotic activity [82][83][84].…”