Complex coacervation behavior and the mechanism between rice glutelin and gum arabic at pH 3.0 studied by turbidity, light scattering, fluorescence spectra and molecular docking

Luo, Weifeng; Huang, Hui; Zhang, Yonghong; Wang, Faxiang; Yu, Jiangnan; Liu, Yongle; Li, Xianghong

doi:10.1016/j.lwt.2021.112084

Cited by 19 publications

(13 citation statements)

References 43 publications

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“…The number of binding sites between the protein and GA was close to 1, which shows that there is only one GA‐binding site on the protein. This is consistent with the results reported by Luo et al ., 30 in which the number of binding sites of some polysaccharides and protein molecules was found to be close to 1.…”

Section: Resultssupporting

confidence: 93%

Effect of enzymatic hydrolysis conditions on structure of soy protein isolate/gum arabic complex and stability of oil‐in‐water emulsion

et al. 2022

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BACKGROUND The emulsifying, antioxidant and foaming properties of soy protein isolate hydrolysates (SPH) can be improved by the addition of gum arabic (GA). We investigated the effects of different hydrolysis conditions on the complexation of SPH and GA, and the effects of the complex on the properties of emulsions. RESULTS Fluorescence spectroscopy showed that the addition of GA had a stronger effect on bromelain and pepsin hydrolysates than trypsin hydrolysate, and therefore had a higher binding constant (KA) and a larger number of binding sites (n). The addition of GA could also improve protein solubility and emulsifying ability. The emulsions prepared with complexes, especially the complex of GA and SPH obtained by pepsin hydrolysis for 3 h, had a high absolute charge value, uniform particle size distribution, stable morphology, and good storage stability. After storage, the emulsification index (CI) of the emulsion only increased to 23.08%; its 1,1‐diphenyl‐2‐picrylhydrazyl (DPPH) free radical scavenging activity was 24.37 ± 1.22% and its 2,2'‐Azinobis‐(3‐ethylbenzthiazoline‐6‐sulphonate) (ABTS+) free radical scavenging activity was largely retained. CONCLUSION During long‐term storage, pepsin‐treated protein (especially protein treated for 3 h) and GA can form a stable emulsion with antioxidant properties. This work provides new ideas for the development of natural and safe emulsifiers that have antioxidant properties and can be stored long‐term and used in the food industry. © 2022 Society of Chemical Industry

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Section: Resultssupporting

confidence: 93%

Effect of enzymatic hydrolysis conditions on structure of soy protein isolate/gum arabic complex and stability of oil‐in‐water emulsion

et al. 2022

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“…As shown in Figure a, when there is no added NaCl, the mixing causes strong complexation between BSA and PDMAEMA 223 , corresponding to the highest turbidity at the optimal DMAEMA/BSA ratio of 17.5/1 (Figure b), as well as coacervates with partial precipitate-like clusters (Figure c,d). Increasing NaCl concentration will weaken the electrostatic interaction between the polymer and protein due to the screening effects, thereby inhibiting the formation of the coacervates accompanied by a decay of the maximum turbidity . This screening effects also interrupt the polymer partition, namely, more proteins and polymers may stay in the top dilution phase rather than involved in the bottom coacervates .…”

Section: Resultsmentioning

confidence: 99%

Effects of Control Factors on Protein–Polyelectrolyte Complex Coacervation

Zhou,

Wan,

Cohen Stuart

et al. 2023

Biomacromolecules

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Protein−polyelectrolyte complex coacervation is of particular interest for mimicking intracellular phase separation and organization. Yet, the challenge arises from regulating the coacervation due to the globular structure and anisotropic distributed charges of protein. Herein, we fully investigate the different control factors and reveal their effects on proteinpolyelectrolyte coacervation. We prepared mixtures of BSA (bovine serum albumin) with different cationic polymers, which include linear and branched polyelectrolytes covering different spacer and charge groups, chain lengths, and polymer structures. With BSA-PDMAEMA [poly(N,N-dimethylaminomethyl methacrylate)] as the main investigated pair, we find that the moderate pH and ionic strength are essential for the adequate electrostatic interaction and formation of coacervate droplets. For most BSA−polymer mixtures, excess polyelectrolytes are required to achieve the full complexation, as evidenced by the deviated optimal charge mixing ratios from the charge stoichiometry. Polymers with longer chains or primary amine groups and a branched structure endow a strong electrostatic interaction with BSA and cause a bigger charge ratio deviation associated with the formation of solid-like coacervate complexes. Nevertheless, both the liquid-and solid-like coacervates hardly interrupt the BSA structure and activity, indicating the safe encapsulation of proteins by the coacervation with polyelectrolytes. Our study validates the crucial control of the diverse factors in regulating protein−polyelectrolyte coacervation, and the revealed principles shall be instructive for establishing other protein-based coacervations and boosting their potential applications.

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“…The complex coacervates are also widely used to encapsulate essential oils and shown to enhance their stability and sustained release. [15][16][17] Gum Arabic has been the polysaccharide of choice to prepare complex coacervates with wider range of proteins (pea proteins, 18 gelatin, 19 rice glutelin, 20 whey proteins 21 and soy proteins 22 ) due to its excellent emulsifying property, solubility in aqueous phase and possession of negative charge for most of the pH range. Gum Arabic-protein complex coacervates are known to possess excellent ability to encapsulate bioactive compounds.…”

Section: Maillard Reaction Has Been Widely To Achieve Covalent Bondin...mentioning

confidence: 99%

Encapsulation of essential oils using hemp protein isolate–gum Arabic complex coacervates and evaluation of the capsules

Liu

Xue

Adhikari

2023

Sustainable Food Technol.

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Complex coacervation behavior and the mechanism between rice glutelin and gum arabic at pH 3.0 studied by turbidity, light scattering, fluorescence spectra and molecular docking

Cited by 19 publications

References 43 publications

Effect of enzymatic hydrolysis conditions on structure of soy protein isolate/gum arabic complex and stability of oil‐in‐water emulsion

Effect of enzymatic hydrolysis conditions on structure of soy protein isolate/gum arabic complex and stability of oil‐in‐water emulsion

Effects of Control Factors on Protein–Polyelectrolyte Complex Coacervation

Encapsulation of essential oils using hemp protein isolate–gum Arabic complex coacervates and evaluation of the capsules

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