Diffusional characteristics of food protein-based materials as nutraceutical delivery systems: A review

Teimouri, Shahla; Kasapis, Stefan; Dokouhaki, Mina

doi:10.1016/j.tifs.2022.02.025

Cited by 17 publications

(5 citation statements)

References 108 publications

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“…According to the Harland equation, the release of TPH, SA as well as INS was due to drug diffusion (correlation coefficient r between 0.672 and 0.987). The MP seemed visually still intact without any visible degradation after 2 h. At intestinal buffer (pH 6.8), TPH, SA and INS were rapidly released from MP due to diffusion of the substance emphasized by polymer degradation [ 61 , 62 , 63 ]. For BD, the release was mainly due to erosion (B > A) of the MP.…”

Section: Resultsmentioning

confidence: 99%

Effect of Molecules’ Physicochemical Properties on Whey Protein/Alginate Hydrogel Rheology, Microstructure and Release Profile

Delanne-Cuménal,

Lainé,

Hoffart

et al. 2024

Pharmaceutics

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The encapsulation of molecules with different physicochemical properties (theophylline, blue dextran, salicylic acid and insulin) in whey protein (WP) and alginate (ALG) microparticles (MP) for oral administration was studied. MP based on WP/ALG were prepared by a cold gelation technique and coated with WP solution after reticulation. Molecules influenced polymer solution viscosity and elasticity, resulting in differences regarding encapsulation efficiency (from 23 to 100%), MP structure and swelling (>10%) and in terms of pH tested. Molecule release was due to diffusion and/or erosion of MP and was very dependent on the substance encapsulated. All the loaded MP were successfully coated, but variation in coating thickness (from 68 to 146 µm) and function of the molecules encapsulated resulted in differences in molecule release (5 to 80% in 1 h). Gel rheology modification, due to interactions between WP, ALG, calcium and other substances, was responsible for the highlighted differences. Measuring rheologic parameters before extrusion and reticulation appeared to be one of the most important aspects to study in order to successfully develop a vector with optimal biopharmaceutical properties. Our vector seems to be more appropriate for anionic high-molecular-weight substances, leading to high viscosity and elasticity and to MP enabling gastroresistance and controlled release of molecules at intestinal pH.

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Section: Resultsmentioning

confidence: 99%

Effect of Molecules’ Physicochemical Properties on Whey Protein/Alginate Hydrogel Rheology, Microstructure and Release Profile

Delanne-Cuménal,

Lainé,

Hoffart

et al. 2024

Pharmaceutics

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“…Developing innovative functional foods that improve public health by incorporating BCs is an exciting area of research (Joye et al., 2015). However, the harsh conditions encountered during food processing and storage, as well as in the digestive system, generally result in BCs being unstable (Teimouri et al., 2022). Encapsulating or entrapping BCs in appropriate delivery systems can enhance their stability and bioavailability against degradation (Qiu et al., 2020).…”

Section: The Nanofibrils In Delivery System Applicationmentioning

confidence: 99%

Nanofibrils of food‐grade proteins: Formation mechanism, delivery systems, and application evaluation

Ban

et al. 2022

Comp Rev Food Sci Food Safe

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Due to the high aspect ratio, appealing mechanical characteristics, and various adjustable functional groups on the surface proteins, food-grade protein nanofibrils have attracted great research interest in the field of food science. Fibrillation, known as a process of peptide self-assembly, is recognized as a common attribute for food-grade proteins. Converting food-grade proteins into nanofibrils is a promising strategy to broaden their functionality and applications, such as improvement of the properties of gelling and emulsifying, especially for constructing various delivery systems for bioactive compounds. Protein source and processing conditions have a great impact on the size, structure, and morphology of nanofibrils, resulting in extreme differences in functionality. With this feature, it is possible to engineer nanofibrils into four different delivery systems, including gels, microcapsules, emulsions, and complexes. Construction of nanofibril-based gels via multiple cross-linking methods can endow gels with special network structures to efficiently capture bioactive compounds and extra mechanical behavior. The adsorption behavior of nanofibrils at the interface is highly complex due to the influence of several intrinsic factors, which makes it challenging to form stabilized nanofibril-based emulsion systems. Based on electrostatic interactions, microcapsules and complexes prepared using nanofibrils and polysaccharides have combined functional properties, resulting in adjustable release behavior and higher encapsulation efficiency.The bioactive compounds delivery system based on nanofibrils is a potential solution to enhance their absorption in the gastrointestinal tract, improve their bioavailability, and deliver them to target organs. Although food-grade protein nanofibrils show unknown toxicity to humans, further research can contribute to broadening the application of nanofibrils in delivery systems.

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“…The gelation of proteins involves two main processes, including protein denaturation/unfolding and then aggregation into a self-supporting structure with a 3-dimensional network [1,3,5]. The gel structure is a suitable medium for encapsulation by protecting sensitive bioactive compounds or nutraceuticals from degradation during food processing and through harsh conditions within the gastrointestinal tract [1,4,6]. In this view, several attempts have been made to produce protein gels of different matrices that serve different purposes in the food industry [2,3,[7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

Effect of Multi-mode Divergent Ultrasound Pretreatment on Hardness, Microstructure and Digestion of Acid-Induced Whey Protein Gels

Cheng,

Shi,

Yeboah

et al. 2024

Preprint

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Whey protein was pretreated with multi-frequency ultrasound in mono, dual, and tri-frequency modes. The effect of multi-frequency ultrasound pretreatment on the hardness, chemical forces, and microstructure of acid-induced whey protein gel was investigated. Whey protein gels pretreated with dual and tri-frequency ultrasound showed higher hardness (p3.35 mm) in those samples were resisted to gastric digestion. Moreover, the tri-frequency ultrasound pretreatment of whey protein gel released the least free amino group during gastric digestion. In contrast, whey protein gel with the mono-frequency ultrasound pretreatment released the highest amount of free amino acid group during intestinal digestion. Findings from this study suggested that gel hardness and network density could modulate the digestion behaviors of protein gels.

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Diffusional characteristics of food protein-based materials as nutraceutical delivery systems: A review

Cited by 17 publications

References 108 publications

Effect of Molecules’ Physicochemical Properties on Whey Protein/Alginate Hydrogel Rheology, Microstructure and Release Profile

Effect of Molecules’ Physicochemical Properties on Whey Protein/Alginate Hydrogel Rheology, Microstructure and Release Profile

Nanofibrils of food‐grade proteins: Formation mechanism, delivery systems, and application evaluation

Effect of Multi-mode Divergent Ultrasound Pretreatment on Hardness, Microstructure and Digestion of Acid-Induced Whey Protein Gels

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