Showing papers on "Bovine serum albumin published in 2016"
TL;DR: The results indicated that AHDMAPPC can bind to BSA and be effectively transported and eliminated in the body, and can be a useful guideline for further drug design.
261 citations
TL;DR: The particular advantages of albumin used in DDSs include ready availability, ease of chemical modification, good biocompatibility, and low immunogenicity.
Abstract: One of the biggest impacts that the nanotechnology has made on medicine and biology, has been in the area of drug delivery systems (DDSs). Many drugs suffer from serious problems concerning insolubility, instability in biological environments, poor uptake into cells and tissues, sub-optimal selectivity for targets and unwanted side effects. Nanocarriers can be designed as DDSs to overcome many of these drawbacks. One of the most versatile building blocks to prepare these nanocarriers is the ubiquitous, readily available and inexpensive protein, serum albumin. Areas covered: This review covers the use of different types of albumin (human, bovine, rat, and chicken egg) to prepare nanoparticle and microparticle-based structures to bind drugs. Various methods have been used to modify the albumin structure. A range of targeting ligands can be attached to the albumin that can be recognized by specific cell receptors that are expressed on target cells or tissues. Expert opinion: The particular advantages of albumin used in DDSs include ready availability, ease of chemical modification, good biocompatibility, and low immunogenicity. The regulatory approvals that have been received for several albumin-based therapeutic agents suggest that this approach will continue to be successfully explored.
222 citations
TL;DR: The experimental results revealed that the fluorescence quenching mechanism of BSA induced atorvastatin was a combined dynamic and static quench, and the main interaction forces were van der Waals force and hydrogen bonding interaction.
201 citations
TL;DR: The results of fluorescence spectroscopy indicated that the fluorescence intensity of BSA was decreased considerably upon the addition of glutathione through a static quenching mechanism, and hydrogen bonding and van der Waals forces were the main interactions in the binding ofglutathione to BSA and the stabilization of the complex.
160 citations
TL;DR: Thermal aggregation of bovine serum albumin has been studied using dynamic light scattering, asymmetric flow field-flow fractionation and analytical ultracentrifugation and analysis of the experimental data shows that at 65°C the stage of protein unfolding and individual stages of protein aggregation are markedly separated in time.
Abstract: Thermal aggregation of bovine serum albumin (BSA) has been studied using dynamic light scattering, asymmetric flow field-flow fractionation and analytical ultracentrifugation. The studies were carried out at fixed temperatures (60°C, 65°C, 70°C and 80°C) in 0.1 M phosphate buffer, pH 7.0, at BSA concentration of 1 mg/ml. Thermal denaturation of the protein was studied by differential scanning calorimetry. Analysis of the experimental data shows that at 65°C the stage of protein unfolding and individual stages of protein aggregation are markedly separated in time. This circumstance allowed us to propose the following mechanism of thermal aggregation of BSA. Protein unfolding results in the formation of two forms of the non-native protein with different propensity to aggregation. One of the forms (highly reactive unfolded form, Uhr) is characterized by a high rate of aggregation. Aggregation of Uhr leads to the formation of primary aggregates with the hydrodynamic radius (Rh,1) of 10.3 nm. The second form (low reactive unfolded form, Ulr) participates in the aggregation process by its attachment to the primary aggregates produced by the Uhr form and possesses ability for self-aggregation with formation of stable small-sized aggregates (Ast). At complete exhaustion of Ulr, secondary aggregates with the hydrodynamic radius (Rh,2) of 12.8 nm are formed. At 60°C the rates of unfolding and aggregation are commensurate, at 70°C the rates of formation of the primary and secondary aggregates are commensurate, at 80°C the registration of the initial stages of aggregation is complicated by formation of large-sized aggregates.
149 citations
TL;DR: In this paper, the role of pH-induced structural change in interface-induced protein aggregation was analyzed using bovine serum albumin (BSA) as a model protein and the results showed that the decrease in pH from 7.0 to 3.0 gradually unfolded the BSA structure to increase the molecular size and the relative content of β-sheet and thus reduced the stability of BSA in the aqueous solution.
141 citations
TL;DR: It is reported that glutaraldehyde cross-linked BSA (or HSA) forms a novel fluorescent biological hydrogel, exhibiting new green and red autofluorescence in vitro and in vivo without the use of any additional fluorescent labels.
Abstract: Because of its good biocompatibility and biodegradability, albumins such as bovine serum albumin (BSA) and human serum albumin (HSA) have found a wide range of biomedical applications. Herein, we report that glutaraldehyde cross-linked BSA (or HSA) forms a novel fluorescent biological hydrogel, exhibiting new green and red autofluorescence in vitro and in vivo without the use of any additional fluorescent labels. UV-vis spectra studies, in conjunction with the fluorescence spectra studies including emission, excitation and synchronous scans, indicated that three classes of fluorescent compounds are presumably formed during the gelation process. SEM, FTIR and mechanical tests were further employed to investigate the morphology, the specific chemical structures and the mechanical strength of the as-prepared autofluorescent hydrogel, respectively. Its biocompatibility and biodegradability were also demonstrated through extensive in vitro and in vivo studies. More interestingly, the strong red autofluorescence of the as-prepared hydrogel allows for conveniently and non-invasively tracking and modeling its in vivo degradation based on the time-dependent fluorescent images of mice. A mathematical model was proposed and was in good agreement with the experimental results. The developed facile strategy to prepare novel biocompatible and biodegradable autofluorescent protein hydrogels could significantly expand the scope of protein hydrogels in biomedical applications.
127 citations
TL;DR: Compared to free Ce6 and Ce6 directly loaded by GO, Ce6–BSA–GO nanohybrids showed enhanced cellular uptake and in vitro release of Ce6, leading to an improved PDT efficiency, indicating that the smart photosensitizer delivery system is promising to improve the stability, biocompatibility, and efficiency of PDT.
Abstract: The inactivation of photosensitizers before they reach the targeted tissues can be an important factor, which limits the efficacy of photodynamic therapy (PDT). Here, we developed co-assembled nanohybrids of graphene oxide (GO) and albumin/photosensitizer that have a potential for protecting the photosensitizers from the environment and releasing them in targeted sites, allowing for an enhanced PDT. The nanohybrids were prepared by loading the pre-assembled nanoparticles of chlorin e6 (Ce6) and bovine serum albumin (BSA) on GO via non-covalent interactions. The protection to Ce6 is evident from the inhibited fluorescence and singlet oxygen generation activities of Ce6–BSA–GO nanohybrids. Importantly, compared to free Ce6 and Ce6 directly loaded by GO (Ce6–GO), Ce6–BSA–GO nanohybrids showed enhanced cellular uptake and in vitro release of Ce6, leading to an improved PDT efficiency. These results indicate that the smart photosensitizer delivery system constructed by co-assembly of GO and albumin is promising to improve the stability, biocompatibility, and efficiency of PDT.
117 citations
TL;DR: Immobilized trypsin (TR) was more stable than the free one and demonstrated higher enzymatic activity at elevated temperatures (45-55°C) and in the alkaline pH region (6-10.5) while Fe3O4 NPs-GA-TR retained about 64% of its initial activity during the same storage period.
114 citations
TL;DR: The results of chemical morphology characterization and in vitro release studies indicated the potential use of BSA NPs as drug carriers in biological systems requiring a fast release of SA.
Abstract: Bovine serum albumin (BSA) is highly water soluble and binds drugs or inorganic substances noncovalently for their effective delivery to various affected areas of the body. Due to the well-defined structure of the protein, containing charged amino acids, albumin nanoparticles (NPs) may allow electrostatic adsorption of negatively or positively charged molecules, such that substantial amounts of drug can be incorporated within the particle, due to different albumin-binding sites. During the synthesis procedure, pH changes significantly. This variation modifies the net charge on the surface of the protein, varying the size and behavior of NPs as the drug delivery system. In this study, the synthesis of BSA NPs, by a desolvation process, was studied with salicylic acid (SA) as the active agent. SA and salicylates are components of various plants and have been used for medication with anti-inflammatory, antibacterial, and antifungal properties. However, when administered orally to adults (usual dose provided by the manufacturer), there is 50% decomposition of salicylates. Thus, there has been a search for some time to develop new systems to improve the bioavailability of SA and salicylates in the human body. Taking this into account, during synthesis, the pH was varied (5.4, 7.4, and 9) to evaluate its influence on the size and release of SA of the formed NPs. The samples were analyzed using field-emission scanning electron microscopy, transmission electron microscopy, Fourier transform infrared, zeta potential, and dynamic light scattering. Through fluorescence, it was possible to analyze the release of SA in vitro in phosphate-buffered saline solution. The results of chemical morphology characterization and in vitro release studies indicated the potential use of these NPs as drug carriers in biological systems requiring a fast release of SA.
104 citations
TL;DR: The calculated results of equilibrium fraction showed that the concentration of free C3G in plasma was high enough to be stored and transported from the circulatory system to reach their target sites to provide their therapeutic effects.
Journal Article•
TL;DR: In this article, the thermal aggregation of bovine serum albumin (BSA) has been studied using dynamic light scattering, asymmetric flow field flow fractionation and analytical ultracentrifugation.
Abstract: Thermal aggregation of bovine serum albumin (BSA) has been studied using dynamic light scattering, asymmetric flow field-flow fractionation and analytical ultracentrifugation. The studies were carried out at fixed temperatures (60°C, 65°C, 70°C and 80°C) in 0.1 M phosphate buffer, pH 7.0, at BSA concentration of 1 mg/ml. Thermal denaturation of the protein was studied by differential scanning calorimetry. Analysis of the experimental data shows that at 65°C the stage of protein unfolding and individual stages of protein aggregation are markedly separated in time. This circumstance allowed us to propose the following mechanism of thermal aggregation of BSA. Protein unfolding results in the formation of two forms of the non-native protein with different propensity to aggregation. One of the forms (highly reactive unfolded form, Uhr) is characterized by a high rate of aggregation. Aggregation of Uhr leads to the formation of primary aggregates with the hydrodynamic radius (Rh,1) of 10.3 nm. The second form (low reactive unfolded form, Ulr) participates in the aggregation process by its attachment to the primary aggregates produced by the Uhr form and possesses ability for self-aggregation with formation of stable small-sized aggregates (Ast). At complete exhaustion of Ulr, secondary aggregates with the hydrodynamic radius (Rh,2) of 12.8 nm are formed. At 60°C the rates of unfolding and aggregation are commensurate, at 70°C the rates of formation of the primary and secondary aggregates are commensurate, at 80°C the registration of the initial stages of aggregation is complicated by formation of large-sized aggregates.
TL;DR: The thermodynamic parameters together with molecular docking study revealed that both van der Waal's forces and hydrogen bonding interaction dominated the formation of the ramiprill-BSA complex and the binding interaction of BSA with ramipril is enthalpy-driven processes due to |ΔH°|>|TΔS°| and ΔG°<0.
Abstract: The binding interaction between a typical angiotensin-converting enzyme inhibitor (ACEI), ramipril, and a transport protein, bovine serum albumin (BSA), was studied in vitro using UV-vis absorption spectroscopy, steady-state fluorescence spectroscopic titration, synchronous fluorescence spectroscopy, three dimensional fluorescence spectroscopy, circular dichroism and molecular docking under the imitated physiological conditions (pH=7.4). The experimental results suggested that the intrinsic fluorescence of BSA was quenched by ramipril thought a static quenching mechanism, indicating that the stable ramipril-BSA complex was formed by the intermolecular interaction. The number of binding sites (n) and binding constant of ramipril-BSA complex were about 1 and 3.50×104M-1 at 298K, respectively, suggesting that there was stronger binding interaction of ramipril with BSA. The thermodynamic parameters together with molecular docking study revealed that both van der Waal's forces and hydrogen bonding interaction dominated the formation of the ramipril-BSA complex and the binding interaction of BSA with ramipril is enthalpy-driven processes due to |ΔH°|>|TΔS°| and ΔG°<0. The spatial distance between ramipril and BSA was calculated to be 3.56nm based on Forster's non-radiative energy transfer theory. The results of the competitive displacement experiments and molecular docking confirmed that ramipril inserted into the subdomain IIA (site I) of BSA, resulting in a slight change in the conformation of BSA but BSA still retained its secondary structure α-helicity.
TL;DR: In this article, the authors investigated the role of the highly anisotropic surface charge distribution of BSA molecules on the process of their adsorption on the surface of SiO 2 using quartz crystal microbalance with energy dissipation mode.
TL;DR: Both spectroscopic techniques demonstrate that there are similar but less spectral changes of BSA for the trypsin attack than for α-chymotrypsin although the substrate/enzyme ratio is taken the same.
TL;DR: In this article, rate constants for the reaction of 4-methylbenzoquinone (4MBQ) with proteins, thiol and amine compounds were determined under pseudo first-order conditions by UV-vis stopped-flow spectrophotometry.
TL;DR: A method based on the atomic force microscope (AFM) to determine pI using minute quantities of proteins and shows that the pI of the 'footprint' of the temporary adhesive proteins secreted by the barnacle cyprid larvae of Amphibalanus amphitrite is in the range 9.6-9.7.
Abstract: Protein charge at various pH and isoelectric point (pI) values is important in understanding protein function. However, often only trace amounts of unknown proteins are available and pI measurements cannot be obtained using conventional methods. Here, we show a method based on the atomic force microscope (AFM) to determine pI using minute quantities of proteins. The protein of interest is immobilized on AFM colloidal probes and the adhesion force of the protein is measured against a positively and a negatively charged substrate made by layer-by-layer deposition of polyelectrolytes. From the AFM force-distance curves, pI values with an estimated accuracy of ±0.25 were obtained for bovine serum albumin, myoglobin, fibrinogen and ribonuclease A over a range of 4.7-9.8. Using this method, we show that the pI of the 'footprint' of the temporary adhesive proteins secreted by the barnacle cyprid larvae of Amphibalanus amphitrite is in the range 9.6-9.7.
TL;DR: It is concluded that the "protein" measured in wastewater samples using standard colorimetric assays often shows false positive results and has little correlation to their real value.
Abstract: Five commercially available assay kits were tested on the same protein sample with the addition of 17 different types of interfering substances typically found in the biological wastewater treatment, and a comparison of the use of these assays with 22 different protein and peptide samples is also presented. It was shown that a wide variety of substances can interfere dramatically with these assays; the metachromatic response was also clearly influenced by different proteinaceous material. Measurement of the “protein” content in the effluent of an anaerobic membrane bioreactor was then carried out using these assay methods. Quantitative results of the “protein” concentration in the different effluent samples, with or without spiked additions of Bovine Serum Albumin (BSA), showed considerable disagreement. We concluded that the “protein” measured in wastewater samples using standard colorimetric assays often shows false positive results and has little correlation to their real value. A new analytical method...
TL;DR: In this paper, the effects of HHP treatments on the conformational (quaternary, tertiary and secondary) structure and the functional properties of a globular water soluble protein, the Bovine Serum Albumin (BSA), were investigated.
Abstract: Non-thermal technologies, such as High Hydrostatic Pressure (HHP), are able to induce extensive changes in the structure of biological macromolecules, namely proteins. HHP treatments disrupt the electrostatic interactions, which stabilize the quaternary and the tertiary structure of the proteins, and activate the reactions of sulfhydryl-disulfide bond exchange. These structural changes result in the dissociation and refolding of proteins during HHP treatments, and consequently in the modification of protein functional properties, namely physicochemical properties (solubility, binding and surfactant properties, water and oil absorption capacity, emulsifying and foaming properties). The technological behavior of the proteins in food preparation, processing, storage, as well as their contribution to determine quality perception of foods mainly depends on these functional properties. This work aims at investigating the effects of HHP treatments on the conformational (quaternary, tertiary and secondary) structure and the functional properties of a globular water soluble protein, the Bovine Serum Albumin (BSA). BSA (50–100 mg/mL) solutions in Sodium Phosphate Buffer were processed at different pressure levels (100–500 MPa) and treatment times (15, 25 min). BSA unfolding and refolding were analyzed in terms of free sulfhydryl (SH) groups, changes of secondary structure, foaming and emulsifying properties. Analyzing the experimental data it can be concluded that the unfolding of BSA samples with a concentration of 50 mg/mL occurred in the pressure range between 100 and 400 MPa. In fact an increased number of the free SH groups as well as an improved foaming and emulsifying ability were detected in the treated samples. Pressure levels above 400 MPa promoted the interactions between adjacent polypeptide chains and the formation of soluble high molecular mass aggregates. The concentration of the protein in the samples, also, controlled the occurrence of unfolding and aggregation. Extensive changes in BSA secondary structure were observed at pressure level above 300 MPa, for longer processing times and higher protein concentrations. In these processing conditions β-sheet aggregates were likely to replace the initial α-helixes. Industrial relevance The paper consists in the study of the Effects of High Hydrostatic Pressure processing (HHP) on the conformational structure and the functional properties of Bovine Serum Albumin. he work proposes an innovative technology for Food Industries that can be widely used for food conservation and to induce protein modifications in the same time. For this reason the technology represents a good tool for the production of hypoallergenic compounds especially in the field of dairy products and infant formula companies.
TL;DR: The spectroscopic evidence showed good binding efficacy of the complexes with BSA and the alterations in the secondary structure of BSA by the Ru(ii) complexes were confirmed by synchronous fluorescence spectra.
Abstract: A series of Ru(II)(η6-p-cymene) complexes (1–4) bearing the general formula [RuCl2(η6-p-cymene)L] (L = monodentate aroylthiourea ligand) has been synthesized and characterized by analytical and various spectroscopic techniques. The neutral monodentate coordination of aroylthiourea with Ru via an S atom was confirmed by single crystal X-ray diffraction study. The complexes were tested for their ability to interact with DNA and protein. The complexes bound with calf thymus DNA (CT DNA) with the intrinsic binding constant value in the order of 104 M−1. The intercalative mode of binding was confirmed by the ethidium bromide (EB) displacement study. The interaction of the complexes with CT DNA was further supported by viscosity measurements and circular dichroic (CD) spectra. The Ru(II) complexes cleaved the supercoiled DNA without the need of any external agent. The spectroscopic evidence showed good binding efficacy of the complexes with BSA (Bovine Serum Albumin). The alterations in the secondary structure of BSA by the Ru(II) complexes were confirmed by synchronous fluorescence spectra. Cytotoxicity examination by MTT assay was carried out in two cancer cell lines (MCF7 and A549) and one non-cancerous cell line (L929). Complex 4 showed significant activity [IC50 = 52.3 (MCF7) and 54.6 (A549) μM] which was comparable with that of similar known complexes. The morphological changes assessed by Hoechst staining revealed that the cell death occurred by apoptosis.
TL;DR: Hydrogen bonds and hydrophobic interactions are the main forces involved in complex formation of NDGA with both the albumins as evaluated from fluorescence and molecular docking results.
Abstract: Exogenous drugs that are used as antidote against chemotheray, inflammation or viral infection, gets absorbed and interacts reversibly to the major serum transport protein i.e. albumins, upon entering the circulatory system. To have a structural guideline in the rational drug designing and in the synthesis of drugs with greater efficacy, the binding mechanism of an antineoplastic and anti-inflammatory drug Nordihydroguaiaretic acid (NDGA) with human and bovine serum albumins (HSA & BSA) were examined by spectroscopic and computational methods. NDGA binds to site II of HSA with binding constant (Kb) ~105 M-1 and free energy (ΔG) ~ -7.5 kcal.mol-1. It also binds at site II of BSA but with lesser binding affinity (Kb) ~105 M-1 and ΔG ~ -6.5 kcal.mol-1. The negative value of ΔG, ΔH and ΔS for both the albumins at three different temperatures confirmed that the complex formation process between albumins and NDGA is spontaneous and exothermic. Furthermore, hydrogen bonds and hydrophobic interactions are the main forces involved in complex formation of NDGA with both the albumins as evaluated from fluorescence and molecular docking results. Binding of NDGA to both the albumins alter the conformation and causes minor change in the secondary structure of proteins as indicated by the CD spectra.
TL;DR: The gram scale synthesis of a COX-2 inhibitor (3-(pyridin-2-ylthio)-1H-indole), regioselectivity and recyclability (up to four cycles) are the additional merits of this cooperative cascade bio-chemocatalytic (BSA-I2) protocol.
Abstract: Cooperative cascade catalysis by bovine serum albumin (BSA)–iodine allows for the first time the performance of C(sp2)–H sulfenylation of indole from readily available thiophenol (–SH bond) via in situ generation/cleavage of disulfide (S–S bond) in air under aqueous conditions, whereas BSA or I2 individually do not permit this two step sequence to occur in the same pot towards C–S bond formation. This green cooperative protocol is extendable to sulfenylation of hydroxyaryls (i.e. 2-naphthol or 4-hydroxycoumarin) with diverse thiols (aryl/heteroaryl) without using any toxic metal catalysts, bases or oxidants, thus rendering the process environmentally and economically reliable. Further, the gram scale synthesis of a COX-2 inhibitor (3-(pyridin-2-ylthio)-1H-indole), regioselectivity and recyclability (up to four cycles) are the additional merits of this cooperative cascade bio-chemocatalytic (BSA–I2) protocol. Moreover, HPLC and ESI-MS provide powerful insights into the mechanistic aspects of the above cascade sulfenylation reaction.
TL;DR: It is demonstrated that only in vivo-matured oocytes maintained correlation between lipid content and active mitochondria and IVM causes changes in mitochondrial and lipid dynamics, which may have negative effects on oocyte development rates and embryo lipid accumulation.
Abstract: Proper oocyte maturation is crucial for subsequent embryo development; however, oocyte mitochondrial and lipid-droplet behaviour are still poorly understood. Although excessive lipid accumulation during in vitro production (IVP) of bovine embryos has been linked with impaired cryotolerance, lipid oxidation is essential for adequate energy supply. Fetal bovine serum (FBS) and bovine serum albumin (BSA) are supplements used during IVP, containing high and low lipid content, respectively. This study aimed to understand how these supplements influence oocyte mitochondrial and lipid behaviour during in vitro maturation (IVM) in comparison to in vivo maturation, as well as their influence on development rates and embryo lipid accumulation during IVP. We demonstrate that only in vivo-matured oocytes maintained correlation between lipid content and active mitochondria. IVM media containing FBS increased total lipid content 18-fold and resulted in higher lipid accumulation in oocytes when compared with media with BSA. IVM using a lower FBS concentration combined with BSA resulted in satisfactory maturation and embryo development and also reduced lipid accumulation in blastocysts. In conclusion, IVM causes changes in mitochondrial and lipid dynamics, which may have negative effects on oocyte development rates and embryo lipid accumulation. Moreover, decreasing FBS concentrations during IVM may reduce embryo lipid accumulation without affecting production rates.
TL;DR: The developed method was successfully applied to determine glycoproteins in egg white of chickens and human urine samples with quantitative spike recoveries from 95% to 104%.
TL;DR: The study describes the development of glucose-sensitive hydrogel and optimization of bovine serum albumin release profile from thehydrogel, and revealed that the swelling of the Hydrogel was influenced by the pH of the medium, and the hydrogels displayed explicit glucose-sensitivity under physiological conditions.
TL;DR: The data of the present study determines the detailed evaluation of BSA adsorption on AgNP along with mechanism, kinetics and isotherm of the Adsorption.
TL;DR: In this article, the interaction of 2-(1-(naphthale-1-ylimino)ethyl)phenol (1), 2-methoxy-4-(((4methoxyphenyl)imino) methyl) phenol (2) with Bovine Serum Albumin (BSA) was examined.
01 Nov 2016
TL;DR: In this paper, Fourier transform infrared spectroscopy was used to obtain information about secondary structure of proteins in different states and also in a whole biological samples, including chicken ovalbumin and bovine serum albumin.
Abstract: Proteins structure is the critical factor for their functioning. Fourier transform infrared spectroscopy provides a possibility to obtain information about secondary structure of proteins in different states and also in a whole biological samples. Infrared spectra of egg white from the untreated and hard-boiled hen's egg, and also of chicken ovalbumin and bovine serum albumin in lyophilic form and in aqueous solution were studied. Lyophilization of investigated globular proteins is accompanied by the decrease of a-helix structures and the increase in amount of intermolecular β-sheets. Analysis of infrared spectrum of egg white allowed to make an estimation of OVA secondary structure and to observe α-to-β structural transformation as a result of the heat denaturation.
TL;DR: VOlut improved the antioxidant capacity of luteolin only against hydroxyl radical and the different coordination may be the cause of the small improvement of some of the tested properties of the flavonoid.
TL;DR: This three-dimensional network system of BPH may be a potential delivery system to improve the stability and bioavailability of functional agents in both food and non-food fields.
Abstract: In this study, a novel hydrogel (BSA–pectin hydrogel, BPH) was prepared via a self-assembly method by using the natural polymers of bovine serum albumin (BSA) and citrus peel pectin (pectin). The rheological properties and gel conformational structures were determined and showed that electrostatic and covalent interactions between BSA and pectin were the main mechanisms for the formation of BPH. The morphological characteristics of BPH included a stable and solid three-dimensional network structure with a narrow size distribution (polydispersity index <0.06). BPH was used as a delivery system to load the functional agent vitamin C (Vc). The encapsulation efficiency (EE) and release properties of Vc from BPH were also investigated. The results revealed that the EE of Vc into BPH was approximately 65.31%, and the in vitro Vc release from BPH was governed by two distinct stages (i.e., burst release and sustained release) in different pH solutions, with release mechanisms involving diffusion, swelling, and er...