Improvement of lactoferrin thermal stability by complex coacervation using soy soluble polysaccharides

Lin, Tiantian; Dadmohammadi, Younas; Davachi, Seyed Mohammad; Torabi, Hooman; Li, Peilong; Pomon, Benjamin; Meletharayil, G. H.; Kapoor, Rohit; Abbaspourrad, Alireza

doi:10.1016/j.foodhyd.2022.107736

Cited by 27 publications

(11 citation statements)

References 45 publications

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“…At pH 6.0 where BSA and PDMAEMA have the optimal charge density, the BSA-PDMAEMA 223 mixture exhibits the highest value of turbidity corresponding to more and larger droplets compared to other pH conditions (Figures c,d and S4 and Table S2), and therefore, pH 6.0 is selected when investigating other control factors. Further increasing pH to 8.0–10.0 not only causes declined protonation of DMAEMA units and consequently the decay of positive charge, but also leads to BSA having the higher absolute value of the net charge, which induces the increased optimal mixing ratio (more polymers are required to fully complex with BSA), as well as the diminished electrostatic interaction between BSA and PDMAEMA, as evidenced by turbidity decay …”

Section: Resultsmentioning

confidence: 99%

“…Further increasing pH to 8.0−10.0 not only causes declined protonation of DMAEMA units and consequently the decay of positive charge, but also leads to BSA having the higher absolute value of the net charge, which induces the increased optimal mixing ratio (more polymers are required to fully complex with BSA), as well as the diminished electrostatic interaction between BSA and PDMAEMA, as evidenced by turbidity decay. 48 Ionic strength is another control factor for regulating the polyelectrolytes coacervation. To do so, the BSA−PDMAE-MA 223 mixtures are prepared in the presence of different NaCl concentrations (0, 10, 20, 50, and 100 mM).…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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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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Section: Resultsmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

Effects of Control Factors on Protein–Polyelectrolyte Complex Coacervation

Zhou,

Wan,

Cohen Stuart

et al. 2023

Biomacromolecules

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“…125 In turn, two denaturation peaks observed at 61 and 90 °C for bLF might be explained by the different thermostabilities of the N-and Clobes and their abilities to release iron. 119,213 As it was mentioned before, the content of bounded iron in LF is strictly dependent on pH; thus the selected medium conditions also have a considerable effect on the protein stability under heating. The denaturation temperatures of apo-and holo-bLFs dissolved at pH 3 were registered at 36 and 49 °C, respectively.…”

Section: G H T S =mentioning

confidence: 91%

The Multifaceted Roles of Bovine Lactoferrin: Molecular Structure, Isolation Methods, Analytical Characteristics, and Biological Properties

Dyrda-Terniuk,

Pomastowski

2023

J. Agric. Food Chem.

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“…Firstly, previous study indicated that the presence of certain polysaccharides can improve the thermal stability of proteins without causing aggregation at high temperature. Therefore, the polysaccharides in soymilk might help to maintain the stability of nano-complexes, contributing to protection of icariin from release during heat treatment [45]. Secondly, the protective effects of the hydrophobic cavity of nano-complexes on icariin presented.…”

Section: Thermal Stabilitymentioning

confidence: 99%

Structure, bioavailability and physicochemical properties of icariin-soymilk nanoparticle

Wang¹,

Wen²,

Jiang³

et al. 2024

Food Science and Human Wellness

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Soymilk is a natural nanocarrier. However, the performance of flavonoid-soymilk nano-complex remains unclear. In this work, icariin-soymilk nano-complexes (ISNCs) were successfully fabricated and characterized. The effects of high-pressure homogenization (HPH) treatment on structure and physicochemical properties of soymilk and nano-complexes were investigated. HPH treatment could significantly improve the surface hydrophobicity and interfacial activity of soymilk. The soymilk with HPH treatment could significantly improve the water solubility (20 folds), thermal stability and bioavailability of icariin. The highest encapsulation efficiency (93.28 %), loading capacity (39.09 µg/mg), ζ-potentia (absolute value, 31.20 mV) and bioavailability (72.14%) were observed in HSI-200 (200 bar of homogenization pressure). While HSI-500 (500 bar of homogenization pressure) showed the smallest particle size (183.73 nm). ISNCs showed a rougher surface and an irregular lamellar structure with large amount of fine particles by using Cryo-SEM, suggesting that icariin was encapsulated in soymilk. These data supplied a novel strategy to improve the performance of icariin in functional foods.

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Improvement of lactoferrin thermal stability by complex coacervation using soy soluble polysaccharides

Cited by 27 publications

References 45 publications

Effects of Control Factors on Protein–Polyelectrolyte Complex Coacervation

Effects of Control Factors on Protein–Polyelectrolyte Complex Coacervation

The Multifaceted Roles of Bovine Lactoferrin: Molecular Structure, Isolation Methods, Analytical Characteristics, and Biological Properties

Structure, bioavailability and physicochemical properties of icariin-soymilk nanoparticle

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