Fabrication and characterization of a succinyl mung bean protein and arabic gum complex coacervate for curcumin encapsulation

Meiguni, Maryam Sadat Mirmohammad; Salami, Maryam; Rezaei, Karamatollah; Aliyari, Mohammad Amin; Ghaffari, Seyed-Behnam; Emam‐Djomeh, Zahra; Kennedy, John F.; Ghasemi, Atiye

doi:10.1016/j.ijbiomac.2022.10.113

Cited by 17 publications

(3 citation statements)

References 57 publications

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“…The turbidity of protein solutions could reflect the solubility and particle size of proteins to a certain extent, which could be used as an ideal macro-indicator for evaluating the degree of protein aggregation. 30 The turbidity of natural BBPI and succinylated BBPI was determined in Figure 1f. The turbidity of BBPI decreased significantly (p < 0.05) as the SA content increased to 5%.…”

Section: Particle Size and ζ-Potentialmentioning

confidence: 99%

Insight into the Stabilization Mechanism of Succinylation Modification on Black Bean Protein Gels: Molecular Conformation, Microstructure, and Gel Properties

Cheng,

Li,

Peng

et al. 2024

J. Agric. Food Chem.

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The objective of this work was to investigate the effect of succinylation treatment on the physicochemical properties of black bean proteins (BBPI), and the relationship mechanism between BBPI structure and gel properties was further analyzed. The results demonstrated that the covalent formation of higher-molecular-weight complexes with BBPI could be achieved by succinic anhydride (SA). With the addition of SA at 10% (v/v), the acylation of proteins amounted to 92.53 ± 1.10%, at which point there was a minimized particle size of the system (300.90 ± 9.57 nm). Meanwhile, the protein structure was stretched with an irregular curl content of 34.30% and the greatest processable flexibility (0.381 ± 0.004). The dense three-dimensional mesh structure of the hydrogel as revealed by scanning electron microscopy was the fundamental prerequisite for the ability to resist external extrusion. The thermally induced hydrogels of acylated proteins with 10% (v/v) addition of SA showed excellent gel elastic behavior (1.44 ± 0.002 nm) and support capacity. Correlation analysis showed that the hydrogel strength and stability of hydrogels were closely related to the changes in protein conformation. This study provides theoretical guidance for the discovery of flexible proteins and their application in hydrogels.

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Section: Particle Size and ζ-Potentialmentioning

confidence: 99%

Insight into the Stabilization Mechanism of Succinylation Modification on Black Bean Protein Gels: Molecular Conformation, Microstructure, and Gel Properties

Cheng,

Li,

Peng

et al. 2024

J. Agric. Food Chem.

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“…Because of the amphiphilicity of proteins, when using complex coacervation to encapsulate hydrophilic (such as oenothein B and garlic extract) or hydrophobic small molecules (such as curcumin), proteins, active molecules, and polysaccharides are usually sequentially mixed to form complexes with a network structure. [160][161][162][163][164][165][166] The phase state of these complexes is related to the structure and properties of the biopolymers. Some researchers have proposed that the stability of bioactive molecules in liquid coacervates may be significantly better than that of amorphous solid precipitates because solid precipitates do not have micron-scale spherical domains (Figure 9B).…”

Section: Encapsulation Of Bioactive Ingredientsmentioning

confidence: 99%

New insights into protein–polysaccharide complex coacervation: Dynamics, molecular parameters, and applications

Zheng,

Van der Meeren,

Sun

2023

Aggregate

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For more than a decade, the discovery of liquid–liquid phase separation within living organisms has prompted colloid scientists to understand the connection between coacervate functionality, phase behavior, and dynamics at a multidisciplinary level. Although the protein–polysaccharide was the first system in which the coacervation phenomenon was discovered and is widely used in food systems, the phase state and relaxation dynamics of protein–polysaccharide complex coacervates (PPCC) have rarely been discussed previously. Consequently, this review aims to unravel the relationship between PPCC dynamics, thermodynamics, molecular architecture, applications, and phase states in past studies. Looking ahead, solving the way molecular architecture spreads to macro‐functionality, that is, establishing the relationship between molecular architecture–dynamics–application, will catalyze novel advancements in PPCC research within the field of foods and biomaterials.

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“…This entrapment of DNA into the protein matrix is completed in the last stage of synthesis. Cationized protein can also be used for making complexes with DNA [ 98 , 99 ].…”

Section: Synthesis Of Protein-based Nanoformulationsmentioning

confidence: 99%

Protein-modified nanomaterials: emerging trends in skin wound healing

Sharda,

Kaur,

Choudhury

2023

Discover Nano

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Prolonged inflammation can impede wound healing, which is regulated by several proteins and cytokines, including IL-4, IL-10, IL-13, and TGF-β. Concentration-dependent effects of these molecules at the target site have been investigated by researchers to develop them as wound-healing agents by regulating signaling strength. Nanotechnology has provided a promising approach to achieve tissue-targeted delivery and increased effective concentration by developing protein-functionalized nanoparticles with growth factors (EGF, IGF, FGF, PDGF, TGF-β, TNF-α, and VEGF), antidiabetic wound-healing agents (insulin), and extracellular proteins (keratin, heparin, and silk fibroin). These molecules play critical roles in promoting cell proliferation, migration, ECM production, angiogenesis, and inflammation regulation. Therefore, protein-functionalized nanoparticles have emerged as a potential strategy for improving wound healing in delayed or impaired healing cases. This review summarizes the preparation and applications of these nanoparticles for normal or diabetic wound healing and highlights their potential to enhance wound healing. Graphical abstract

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Fabrication and characterization of a succinyl mung bean protein and arabic gum complex coacervate for curcumin encapsulation

Cited by 17 publications

References 57 publications

Insight into the Stabilization Mechanism of Succinylation Modification on Black Bean Protein Gels: Molecular Conformation, Microstructure, and Gel Properties

Insight into the Stabilization Mechanism of Succinylation Modification on Black Bean Protein Gels: Molecular Conformation, Microstructure, and Gel Properties

New insights into protein–polysaccharide complex coacervation: Dynamics, molecular parameters, and applications

Protein-modified nanomaterials: emerging trends in skin wound healing

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