Characterization of binding interactions of anthraquinones and bovine β-lactoglobulin

Xu, Haoxie; Lu, Yuqin; Zhang, Tingting; Liu, Ke; Liu, Lizhong; He, Zhendan; Xu, Bingqi; Wu, Xuli

doi:10.1016/j.foodchem.2018.12.077

Cited by 51 publications

(27 citation statements)

References 28 publications

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“…However, ultrasound generated acoustic cavitation, resulted in three times greater binding constant (ka) of casein-emodin complexes than heat treatment alone. This ka value was close to the previously reported value of binding emodin and βLG or tyrosinase and β casein and epigallocatechin [174,175].…”

Section: Researchers Cohen and Hahamsupporting

confidence: 90%

Casein Micelles as an Emerging Delivery System for Bioactive Food Components

Sadiq

Gill

Chandrapala

2021

Foods

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Bioactive food components have potential health benefits but are highly susceptible for degradation under adverse conditions such as light, pH, temperature and oxygen. Furthermore, they are known to have poor solubilities, low stabilities and low bioavailabilities in the gastrointestinal tract. Hence, technologies that can retain, protect and enable their targeted delivery are significant to the food industry. Amongst these, microencapsulation of bioactives has emerged as a promising technology. The present review evaluates the potential use of casein micelles (CMs) as a bioactive delivery system. The review discusses in depth how physicochemical and techno-functional properties of CMs can be modified by secondary processing parameters in making them a choice for the delivery of food bioactives in functional foods. CMs are an assembly of four types of caseins, (αs1, αs2, β and κ casein) with calcium phosphate. They possess hydrophobic and hydrophilic properties that make them ideal for encapsulation of food bioactives. In addition, CMs have a self-assembling nature to incorporate bioactives, remarkable surface activity to stabilise emulsions and the ability to bind hydrophobic components when heated. Moreover, CMs can act as natural hydrogels to encapsulate minerals, bind with polymers to form nano capsules and possess pH swelling behaviour for targeted and controlled release of bioactives in the GI tract. Although numerous novel advancements of employing CMs as an effective delivery have been reported in recent years, more comprehensive studies are required to increase the understanding of how variation in structural properties of CMs be utilised to deliver bioactives with different physical, chemical and structural properties.

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Section: Researchers Cohen and Hahamsupporting

confidence: 90%

Casein Micelles as an Emerging Delivery System for Bioactive Food Components

Sadiq

Gill

Chandrapala

2021

Foods

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“…2). This observation is in good agreement with in silico predictions, indicating that binding sites other than β-barrel, may include (1) a hydrophobic pocket close to dimer interface in a groove between the α-helix and the β-barrel (Yang et al, 2007;Domínguez-Ramírez et al, 2013) or (2) the outer surface near Trp19 and Arg124 (Sahihi et al, 2013;Liu et al, 2017;Xu et al, 2019). It is highly probable that different polar aromatic compounds, e.g.…”

Section: Structure Of L39k and F105a Mutantssupporting

confidence: 86%

“…Although presented here crystal structure of I56F variant in complex with tetracaine is the first crystallographic evidence of a new binding site on the BLG surface near Arg124 and Trp19, this site requires two BLG molecules and is available only in the crystalline phase. Nevertheless, based on spectroscopic studies, it was proposed that some aromatic compounds were bound at a similar location (Liang & Subirade, 2012;Xu et al, 2019). In the presence of TET, the molecular packing in crystals of the I56F variant was different than that observed for other BLG mutants.…”

Section: Structure Of L39k and F105a Mutantsmentioning

confidence: 97%

Interactions of new lactoglobulin variants with tetracaine: crystallographic studies of ligand binding to lactoglobulin mutants possessing single substitution in the binding pocket

et al. 2021

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β-Lactoglobulin (BLG) like other lipocalins can be modified by mutagenesis to re-direct its ligand binding properties. Local site-directed mutagenesis was used to change the geometry of the BLG ligand binding pocket and therefore change BLG ligand preferences. The presented studies are focused on previously described mutants L39Y, I56F, L58F, F105L, and M107L and two new BLG variants, L39K and F105A, and their interactions with local anesthetic drug tetracaine. Binding of tetracaine to BLG mutants was investigated by X-ray crystallography. Structural analysis revealed that for tetracaine binding, the shape of the binding pocket seems to be a more important factor than the substitutions influencing the number of interactions. Analyzed BLG mutants can be classified according to their binding properties to variants: capable of binding tetracaine in the β-barrel (L58F, M107L); capable of accommodating tetracaine on the protein surface (I56F) and unable to bind tetracaine (F105L). Variants L39K, L39Y, and F105A, had a binding pocket blocked by endogenous fatty acids. The new tetracaine binding site was found in the I56F variant. The site localized on the surface near Arg124 and Trp19 was previously predicted by in silico studies and was confirmed in the crystal structure.

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“…At present, there have not been reports on the suitable surface-active compound for the adsorption of anthraquinones at the gas-liquid interface. However, a large number of studies have confirmed that anthraquinones have good protein binding affinity [15][16][17]. Thus we propose that proteins in Semen Cassiae may also have good interactions with anthraquinones.…”

Section: Introductionmentioning

confidence: 71%

Separation of Protein-Binding Anthraquinones from Semen Cassiae Using Two-Stage Foam Fractionation

Ding

Wang²,

Yue

et al. 2019

Processes

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Anthraquinones are compounds of high medicinal value in many plants. Based on their good protein binding affinity, foam fractionation was attempted to separate them using proteins in the aqueous extract of Semen Cassiae as collectors. Firstly, the interaction between anthraquinones and Semen Cassiae proteins has been analyzed by the Stem–Volmer equation with physcion as a standard. The results show that physcion had good interaction with the proteins via hydrophobic forces. More importantly, the proteins effectively assisted the foam fractionation of several anthraquinones including aurantio-obtusifolin, aloe-emodin, rhein, emodin, chrysophanol, and physcion. On this basis, a two-stage foam fractionation technology was developed for process intensification using a foam fractionation with vertical sieve trays (VSTs). VSTs, initial feed concentration of total anthraquinones, temperature, volumetric air flow rate and pore diameter of gas distributor had significant effects on enrichment ratio and recovery yield of anthraquinones. Under suitable conditions, the enrichment ratio of total anthraquinones reached 47.0 ± 4.5 with a concentration of 939 ± 94 mg/L in the foamate while their total recovery percentage reached more than 47.7%. In addition, foam fractionation also increased the purity and hydroxyl radical scavenging activity of total anthraquinones. The results had significant implications for the separation of anthraquinones from Semen Cassiae.

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Characterization of binding interactions of anthraquinones and bovine β-lactoglobulin

Cited by 51 publications

References 28 publications

Casein Micelles as an Emerging Delivery System for Bioactive Food Components

Casein Micelles as an Emerging Delivery System for Bioactive Food Components

Interactions of new lactoglobulin variants with tetracaine: crystallographic studies of ligand binding to lactoglobulin mutants possessing single substitution in the binding pocket

Separation of Protein-Binding Anthraquinones from Semen Cassiae Using Two-Stage Foam Fractionation

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