Beta-lactoglobulin-based encapsulating systems as emerging bioavailability enhancers for nutraceuticals: a review

Teng, Zi; Xu, Ruoyang; Wang, Qin

doi:10.1039/c5ra01814e

Cited by 91 publications

(49 citation statements)

References 107 publications

(110 reference statements)

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“…The binding affinity of these new calix[4]arenes toward β‐lactoglobulin (BLG) as a model protein was investigated by using fluorescence spectrophotometric methods. We used BLG as a model protein because of its natural abundance, high stability, and numerous physiological and pharmacological functions . Because these designed molecules have multifunctional structures, associative, non‐covalent binding forces, such as hydrogen bonding, hydrophobic interaction, and van der Waals interactions, are expected.…”

Section: Introductionmentioning

confidence: 99%

“…We used BLG as a model protein because of its natural abundance, high stability, and numerous physiological and pharmacological functions. [28] Because these designed molecules have multifunctional structures, associative, non-covalent binding forces, such as hydrogen bonding, hydrophobic interaction, and van der Waals interactions, are expected. We believe that six amide groups are necessary for the formation of hydrogen bonding between ligand and protein.…”

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confidence: 99%

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An Efficient Multi‐Component Synthesis of Highly Functionalized Calix[4]arenes with Pronounced Binding Affinity toward β‐Lactoglobulin

et al. 2016

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A facile and convenient approach for the synthesis of multi‐functionalized calix[4]arenes through multi‐component reactions is described. A series of five new calix[4]arene‐hexaamide derivatives were synthesized, and their structures were elucidated by means of spectroscopic data. The value of this method lies in its operational simplicity, mild reaction conditions, structural diversity of products, and good yields. Furthermore, fluorescence studies demonstrated considerable binding affinity of these new calix[4]arenes toward β‐lactoglobulin protein.

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Section: Introductionmentioning

confidence: 99%

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confidence: 99%

An Efficient Multi‐Component Synthesis of Highly Functionalized Calix[4]arenes with Pronounced Binding Affinity toward β‐Lactoglobulin

et al. 2016

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“…The chemical and enzymatic hydrolyses, the acylation [21], cationization [21,78] and Maillard reactions [12,19,77] are the best chemical treatments to improve their functionality [12,43]. For instance, Nesterenko et al [46] studied native and modified soybean and sunflower seed proteins to encapsulate α-tocopherol by spray drying.…”

Section: Structural Changes In Proteins: a Strategy To Enhance Their mentioning

confidence: 99%

Vegetable Proteins: Non-sensitizing Encapsulation Agents for Bioactive Compounds

Quiroz¹,

Durán²,

Ciro-Gómez³

et al. 2017

Allergen

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Plant-derived proteins are remarkable macromolecules of scientific interest because they represent an alternative to the animal-derived proteins and petroleum-derived polymers. Many food proteins especially those derived from animal sources could act as antigens in humans. For instance, milk proteins extracted from cows may cause food intolerance during infancy. Further, soybean, peanuts, tree nuts, fish, crustacean shellfish and egg proteins may act as antigens in 90% of children. Since the GI tract is permeable to intact antigens the oral intake of these proteins may generate gastrointestinal (50-80%), cutane ous (20-40%) and respiratory symptoms (4-25%). Most of these allergens are water-soluble glycoproteins that are resistant to acids and enzymes. Usually, these proteins have a small molecular weight (10,000-60,000 kDa), water solubility, glycosylation residues, and a rela tive resistance to heat and digestion. Allergenicity is less frequent in vegetable proteins due to their less flexible and non-compact structure. Allergenicity is also related to the resistance to proteolysis, post-translational glycosylation, presence of epitopes, and enzy matic proteolysis. Moreover, proteins serve as a coating material if structural modifica tions in the protein, either by physical, chemical or enzymatic mechanisms are conducted. As a result, their allergenicity is reduced, and their functional properties are enhanced.

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“…Achieving an increase in encapsulation efficiency from 82.6% to 94.8% in the case of soybeans and from 79.7% to 99.5% in the case of sunflower seed proteins treated by acylation. They concluded that the structural modification of these proteins increased the affinity between the active ingredient and the coating material, improving the encapsulation process, the hydration and the net charge of the protein (Nedovic and Willaert, 2013;Zhang, Tan, Abbas et al, 2014;Carbonaro et al, 2014;Teng et al, 2015).…”

Section: Cationization Reactionmentioning

confidence: 99%

Wheatgrass juice, Sensory analyses, Novel food, Functional food

Quiroz¹,

Rojas²,

Ciro-Gómez³

2018

Food Res.

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Proteins from plant sources are macromolecules of industrial interest due to its high availability, biodegradability, renewable character and functional properties such as biocompatibility, good amphiphilic properties, water solubility, foaming, emulsifying, gelling and film-forming abilities. In this scenario, these macromolecules have a high applicability in various emulsification stabilization processes, and have a potential use as a wall-forming material for the encapsulation processes of active ingredients. Currently, proteins extracted from soybean, pea, sunflower, rice and wheat seeds have already been studied as versatile stabilizers and emulsion coatings by coacervation and encapsulation processes by spray-drying. However, the capsule-forming ability of these macromolecules is enhanced by physical, chemical or enzymatic changes in their structure, favoring the interactions with the core material, the solvent, and increase of the encapsulation efficiency and its versatility in other encapsulation techniques.

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Beta-lactoglobulin-based encapsulating systems as emerging bioavailability enhancers for nutraceuticals: a review

Abstract: Encapsulating systems prepared with beta-lactoglobulin, the major component of whey protein, may serve as versatile bioavailability enhancers for poorly absorbed nutraceuticals.

Cited by 91 publications

References 107 publications

An Efficient Multi‐Component Synthesis of Highly Functionalized Calix[4]arenes with Pronounced Binding Affinity toward β‐Lactoglobulin

An Efficient Multi‐Component Synthesis of Highly Functionalized Calix[4]arenes with Pronounced Binding Affinity toward β‐Lactoglobulin

Vegetable Proteins: Non-sensitizing Encapsulation Agents for Bioactive Compounds

Wheatgrass juice, Sensory analyses, Novel food, Functional food

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