Alcalase-hydrolyzed insoluble soybean meal hydrolysate aggregates: Structure, bioactivity, function properties, and influences on the stability of oil-in-water emulsions.

We studied the influences of hydrolysis time on the structure, functional properties, and emulsion stability of insoluble soybean meal hydrolysate aggregates (ISMHAs). We assume that the ISMHAs produced by soybean meal can be used as emulsifiers to prepare stable emulsions. The molecular weights of these ISMHAs were below 53 kDa. After hydrolysis, a decrease in α-helices and an increase in random coils indicated that the soybean meal proteins were unfolding. Moreover, the fluorescence intensity, UV absorption, and surface hydrophobicity of ISMHAs increased. These results would contribute to their antioxidant activity and functional properties. Additionally, the 90-min ISMHA sample exhibited the highest ABTS+• scavenging activity (80.02 ± 4.55 %), foaming stability (52.92 ± 8.06 %), and emulsifying properties (emulsifying activity index of 97.09 m2/g; emulsifying stability index of 371.47 min). The 90-min ISMHA emulsion exhibited the smallest particle size and excellent storage stability. Soybean meal peptide by-product emulsifier has potential for sustainable application.

Structural and interfacial properties of acetylated Millettia speciosa Champ polysaccharide and stability evaluation of the resultant O/W emulsion containing ß-carotene.

The aim of this study was to investigate the effects of acetylation modification on the structural, interfacial and emulsifying properties of Millettia speciosa Champ polysaccharide (MSCP). Besides, the influence of acetylation modification on the encapsulation properties of polysaccharide-based emulsion was also explored. Results indicated that modification resulted in a prominent reduction in molecular weight of MSCP and the interfacial layer thickness formed by acetylated MSCP (AC-MSCP) was also decreased, but the adsorption rate and ability of AC-MSCP to reduce interfacial tension were improved. AC-MSCP formulated emulsion possessed smaller droplet size (6.8 µm) and exhibited better physical stability under stressful conditions. The chemical stability of ß-carotene was also profoundly enhanced by AC-MSCP fabricated emulsion. Moreover, AC-MSCP improved lipids digestion extent, thus facilitating the formation of micelle and increasing bioaccessibility of ß-carotene. This study provided insights for rational modification of polysaccharide-based emulsifier and designing delivery system for chemically labile hydrophobic bioactive components.

Study on the structural characteristics and emulsifying properties of chickpea protein isolate-citrus pectin conjugates prepared by Maillard reaction.

Chickpea protein isolate (CPI) typically exhibits limited emulsifying properties under various food processing conditions, including pH variations, different salt concentrations, and elevated temperatures, which limits its applications in the food industry. In this study, CPI-citrus pectin (CP) conjugates were prepared through the Maillard reaction to investigate the influence of various CP concentrations on the structural and emulsifying properties of CPI. With the CPI/CP ratio of 1:2, the degree of graft reached 35.54 %, indicating the successful covalent binding between CPI and CP. FT-IR and intrinsic fluorescence spectroscopy analyses revealed alterations in the secondary and tertiary structures of CPI after glycosylation modification. The solubility of CPI increased from 81.39 % to 89.59 % after glycosylation. Moreover, freshly prepared CPI emulsions showed an increase in interfacial protein adsorption (70.33 % to 92.71 %), a reduction in particle size (5.33 µm to 1.49 µm), and a decrease in zeta-potential (-34.9 mV to -52.5 mV). Simultaneously, the long-term stability of the emulsions was assessed by employing a LUMiSizer stability analyzer. Furthermore, emulsions prepared with CPI:CP 1:2 exhibited excellent stability under various environmental stressors. In conclusion, the results of this study demonstrate that the glycosylation is a valuable approach to improve the emulsifying properties of CPI.

Fabrication of high-preformance emulsifier from conjugating maltodextrin onto myofibrillar protein peptide with microwave- ultrasound synergy.

In this study, we systematically investigated the emulsifying capabilities of myofibrillar protein (MP)- and MP peptide (MPP)-based conjugates synthesized through intensification techniques: water bath (WB), microwave, ultrasound, and the combined ultrasound-microwave (UM) methods. Compared with WB, microwave, and ultrasound treatments, the combined UM treatment greatly promoted the glycation reaction because ultrasound and microwave mutually reinforced modification effects. The resultant conjugate structure tended to unfold with more flexible conformation and homogeneous morphology. Moreover, the emulsifying properties of conjugates developed with single and combined ultrasound-assisted glycation displayed substantial improvement, and pre-hydrolysis further enhanced these performances, as observed in the Principal Component Analysis as well. Remarkably, MPP grafted by maltodextrin with the assistance of a combined UM field produced the smallest and most uniform emulsion system, positioning it as the most efficient emulsifier among all the fabricated glycoconjugates. Our study highlighted the potential of synergistically applying ultrasound and microwave techniques to develop a well-performance glycation with an ideal conjugate structure, in which they would be associated into a strong film that provided the robust physical barrier, creaming stability, heat retention, and oxidation resistance. These findings offered a basis for better utilizing complex ultrasonic technology to develop novel and improved MP-based food products.

Modification mechanism of soybean protein isolate-soluble soy polysaccharide complex by EGCG through covalent and non-covalent interaction: Structural, interfacial, and functional properties.

Soybean protein isolate was modified with polysaccharides and polyphenols to prepare a natural emulsifier with antioxidant capacity. Physicochemical, structural, interfacial, and functional properties of SPI-SSPS complex were investigated after covalent and non-covalent interacted with EGCG. SPI-SSPS-EGCG ternary complex with low EGCG concentrations (0.0625 and 0.125 mg/mL) showed a significant increase in absolute potential value and a decrease in turbidity. EGCG destroyed the original rigid structure of SPI-SSPS complex, and the covalent complexes had an ordered structure, while the non-covalent interaction resulted in disordered. The ternary complex with high EGCG concentrations (0.25 and 0.5 mg/mL) exhibited stronger EGCG binding capacity and lower surface hydrophobicity, which in turn affected its interfacial properties. The EAI and ESI of SPI-SSPS-EGCG covalent complex increased significantly, while the non-covalent complex had a significant change in EAI but no significant change in ESI with increasing EGCG concentration. The ternary complex showed significantly enhanced antioxidant capacity. The SPI-SSPS-EGCG ternary complex, with excellent antioxidant capacity and emulsifying property, making it suitable for emulsion delivery systems.

Dual functionality of diacylglycerols in water-in-oil emulsion gel systems.

Distearin (DS) can be used as an emulsifier, due to its surface activity derived from the amphiphilic nature of the molecule, moreover, it can also crystallize and form a 3D crystal network that can induce oil gelation. The current research aimed to examine the ability to combine both emulsifying and oil gelation properties to structure and stabilize water-in-oil emulsion gel system. Different water contents and DS concentrations produce emulsion gels with different textural attributes while incorporating up to 30% of water in a 15% wt. DS-based oleogel resulted in stable white gels. Microscopy imaging confirmed the formation of a water-in-oleogel type emulsion gel characterized by DS crystallization in the continuous phase and at the interface through Pickering mechanism. A positive relation was observed between the G' and hardness values and water content, suggesting gel strengthening resulted from interactions between the DS crystals at the interface and the continuous phase, as suggested by the active filler theory. Thermal analysis revealed two broad melting events at the temperature range of 42.2-44.9 °C and 55.9-58.6 °C for emulsion gels with 10-30% water content, suggesting initial melting of ß' polymorph and transition to ß during melting, which was confirmed by XRD. The results showed that homogenization significantly improved the oil retention of the gels due to increased crystal surface area, while water addition slightly reduced it. Compared with traditional emulsions or oleogels, this water-in-oil gel system demonstrated prolonged stability and enhanced mechanical properties due to the dual functionality of DS at the water/oil interface and bulk.

The effects of resonance acoustic mixing modulation on the structural and emulsifying properties of pea protein isolate.

The effects of resonant acoustic mixing (RAM) with different treatment times (0, 5, 10, 15, 20 and 30 min) on the structural and emulsifying properties of pea protein isolate (PPI) were investigated for the first time. Increasing the RAM treatment time from 0 to 20 min decreased the α-helix/ß-sheet ratio and particle size of the PPI samples by 37.84 % and 46.44 %, respectively, accompanied by an increase in solubility from 54.79 % to 71.80 % (P < 0.05). Consequently, the emulsifying activity index of PPI (from 10.45 m2/g to 14.2 m2/g) and the physical stability of RAM-PPI emulsions were effectively enhanced, which was confirmed by the small and uniformly distributed oil droplets in the micrographs of the emulsions. However, excessive RAM treatment (30 min) diminished the effectiveness of the aforementioned improvements. Therefore, obviously enhanced solubility and emulsifying properties of PPI can be attained through proper RAM treatment (15-20 min).

High-pressure microfluidization enhanced the stability of sodium caseinate-EGCG complex-stabilized fish oil emulsion.

Improving the emulsion-stabilizing effect of protein by chemical or physical modification has been paid much attention recently. Here, sodium caseinate (CS) was treated by high-pressure-microfluidization (HPM) under 0-100 MPa, and was further complexed with (-)-epigallocatechin-3-gallate (EGCG) to form an excellent emulsifier that stabilized fish oil emulsions. Results showed that HPM treatment (especially 80 MPa) significantly changed the secondary structure of CS, and 80 MPa-PCS-EGCG had the best emulsifying and antioxidant activities. In addition, after HPM treatment and EGCG bonding, CS formed a thicker interface layer on the surface of oil droplets, which could better protect the fish oil from the influence by oxygen, temperature and ion concentration. Moreover, the fish oil emulsion stabilized by PCS-EGCG complex significantly delayed the release of free fatty acids subjected to in vitro digestion. Conclusively, HPM-treated CS-EGCG complex could be a potential emulsifier to improve the stability of fish oil emulsions.

Food emulsions stabilized by proteins and emulsifiers: A review of the mechanistic explorations.

The stability of food emulsions is the basis for other properties. During their production and processing, emulsions tend to become unstable due to their thermodynamic instability, and it is usually necessary to add emulsifiers and proteins to stabilize emulsions. It becomes crucial to study the intrinsic mechanisms of emulsifiers and proteins and their joint stabilization of food emulsions. This paper summarizes the research on intrinsic mechanisms of food emulsions stabilized by emulsifiers and proteins in recent years. The destabilization and stabilization of emulsions are related to the added surfactants. The properties, type, and concentration of emulsifiers determine the stability of emulsions, and the emulsifiers can be classified into different types (e.g., ionic or nonionic, solid or liquid) according to their properties and sources. The physicochemical properties of proteins (e.g., spatial conformation, hydrophobicity) and the composition of proteins can also determine the stability of emulsions, and emulsions stabilized by emulsifiers and proteins together not only depend on these factors but also have a great relationship with the mutual combination and competition between the two. The instability and stability of emulsions are related to factors such as interfacial interaction forces, the rheological nature of the interface, and the added surfactant.

Development and characterization of nanostructured lipid carriers for cannabidiol delivery.

This study evaluated the physicochemical characteristics of nanostructured lipid carriers (NLCs) as a potential vehicle for cannabidiol (CBD), a lipophilic molecule with great potential to promote health benefits. NLCs were produced using hemp seed oil and fully-hydrogenated soybean oil at different proportions. The emulsifiers evaluated were soybean lecithin (SL), Tween 80 (T80) and a mixture of SL:T80 (50:50). CBD was tested in the form of CBD-rich extract or isolate CBD, to verify if it affects the NLCs characteristics. Based on particle size and polydispersity, SL was considered the most suitable emulsifier to produce the NLCs. All lipid proportions evaluated had no remarkable effect on the physicochemical characteristics of NLCs, resulting in CBD-loaded NLCs with particle size below 250 nm, high CBD entrapment efficiency and CBD retention rate of 100% for 30 days, demonstrating that NLCs are a suitable vehicle for both CBD-rich extract or isolate CBD.

Noncovalent interactions between biomolecules facilitated their application in food emulsions' construction: A review.

The use of biomolecules, such as proteins, polysaccharides, saponins, and phospholipids, instead of synthetic emulsifiers in food emulsion creation has generated significant interest among food scientists due to their advantages of being nontoxic, harmless, edible, and biocompatible. However, using a single biomolecule may not always meet practical needs for food emulsion applications. Therefore, biomolecules often require modification to achieve ideal interfacial properties. Among them, noncovalent interactions between biomolecules represent a promising physical modification method to modulate their interfacial properties without causing the health risks associated with forming new chemical bonds. Electrostatic interactions, hydrophobic interactions, and hydrogen bonding are examples of noncovalent interactions that facilitate biomolecules' effective applications in food emulsions. These interactions positively impact the physical stability, oxidative stability, digestibility, delivery characteristics, response sensitivity, and printability of biomolecule-based food emulsions. Nevertheless, using noncovalent interactions between biomolecules to facilitate their application in food emulsions still has limitations that need further improvement. This review introduced common biomolecule emulsifiers, the promotion effect of noncovalent interactions between biomolecules on the construction of emulsions with different biomolecules, their positive impact on the performance of emulsions, as well as their limitations and prospects in the construction of biomolecule-based emulsions. In conclusion, the future design and development of food emulsions will increasingly rely on noncovalent interactions between biomolecules. However, further improvements are necessary to fully exploit these interactions for constructing biomolecule-based emulsions.

Enhanced emulsification performance and interfacial properties of Janus-like rapeseed cruciferin through asymmetric acylation modification.

Plant protein emulsifiers, particularly rapeseed protein isolate with its superior amino acid composition and predominantly globular protein, have captured significant interest in the food industry. Nonetheless, the application of these proteins has been stymied by their lackluster emulsification properties. Addressing this challenge, our study implements an innovative asymmetric acylation technique to modify the surface of rapeseed cruciferin (RC), morphing it into a structure resembling Janus nanoparticles. This alteration amplifies the emulsification prowess of RC by a remarkable 2.7 times compared to its natural form, and 1.43 times over its conventionally acylated counterpart. The asymmetrically acylated RC, marked by a distinctive three-phase contact angle of 90.4°, manifests an outstanding amphiphilic character. Moreover, it surpasses both the natural and conventionally acylated RC in terms of diffusion, penetration, and rearrangement rates, as well as protein concentration at the oil-water interface. Compared to commonly used emulsifiers in the food industry, such as lecithin and soy protein, the asymmetrically acylated RC stands out, stabilizing emulsions with the tiniest particle size and effectively staving off emulsion stratification over a longer duration. This study underscores that asymmetric acylation serves as a reliable methodology for producing efficient plant protein emulsifiers, considerably amplifying their utility in the food industry.

Developing biopolymer-stabilized emulsions for improved stability and bioaccessibility of lutein.

Lutein is essential for infant visual and cognitive development but has low stability and solubility. This study aimed to enhance the stability and bioaccessibility of lutein using oil-in-water emulsions stabilized with biopolymers. Commercially available octenylsuccinylated (OS) starches, including capsule TA® (CTA), HI-CAP®100 (HC), and Purity Gum® 2000 (PG), along with gum Arabic (GA) variants Ticaloid acacia Max® (TAM), TICAmulsion® 3020 (TM), and pre-hydrate gum Arabic (PHGA), were chosen as emulsifiers. By screening the effect of biopolymer concentration and oil volume fraction (Φ), emulsions stabilized with CTA, HC, or TM at 20% and 30% (w/v) concentration and 70% Φ exhibited a gel-like structure and were selected for further assessments. After a week at 25 °C, emulsions stabilized by CTA and HC showed no significant change in droplet size, while TM emulsion exhibited a 1.58-fold increase. At 45 °C, all emulsions exhibited increase in droplet size. Lutein retention is higher in CTA emulsions at both storage temperatures than free lutein. In vitro bioaccessibility of all lutein emulsions was higher than that of free lutein. These findings highlight the superior stability and bioaccessibility of the lutein emulsion stabilized by OS starch, positioning it as a promising carrier to broaden lutein applications in infant foods.

Enhancing the Thermal Stability of Zein Particle-Stabilized Aeratable Emulsions Through Genipin-Protein Cross-Linking and Its Possible Mechanism of Action.

Protein particle-stabilized emulsions often lack thermal stability, impacting their industrial use. This study investigated the effects of genipin (GP)-zein cross-linked particles with varying GP-to-protein weight ratios (0/0.02/0.1:1) on emulsion thermal stability. Enhanced stability was observed at the GP level of 0.1. Heat treatment increased the covalent cross-linking in raw particles and emulsions. Isolated particles from heated emulsions grew in size (micrometer scale) with higher GP levels, unlike heated raw particles (nanoscale). GP-protein cross-linking reduced the droplet-droplet and particle-emulsifier interactions in the heated emulsion. Spectroscopic analysis and electrophoresis revealed that GP-zein cross-linking increased protein structural stability and inhibited nondisulfide and non-GP cross-linking reactions in heated emulsions. The GP-zein bridges between particles at the oil-water interface create strong connections in the particle layer (shell), referred to as "particle-shell locking", enhancing the thermal stability of emulsion significantly. This insight aids the future design of protein-particle-based emulsions, preserving properties like aeratability during thermal processing.

Effect of synergism of sucrose ester and xanthan gum on the stability of walnut milk.

BACKGROUND: Single emulsifiers have an effect on the stability of plant protein drinks, giving some improvement. Emulsifiers are more effective in maintaining emulsion stability when combined with polysaccharides such as xanthan gum. In this paper, we studied the food-grade emulsifier sucrose ester and measured the average particle size, polydispersity value, zeta potential, microrheological properties, microstructure and creaming index related to walnut protein emulsion by constructing a walnut protein emulsion simulation system. SDS-PAGE and low-field NMR were used to analyze the relative molecular masses of emulsions and the water distribution of emulsions, respectively, to further investigate the synergistic effects of sucrose esters and xanthan gum on the ease of emulsification and intrinsic mechanisms of different molecular weight proteins of walnut protein emulsions. RESULTS: The results indicate that the synergistic effect of sucrose esters and xanthan gum was to stabilize emulsions better than single emulsifiers. Xanthan gum and protein may form protein-polysaccharide complexes, as well as the hydrophobic interaction between sucrose ester and xanthan gum. The properties of xanthan gum can improve the stability of the emulsion by affecting the mechanical properties of walnut protein emulsion, and the combination of sucrose ester and xanthan gum can better stabilize large protein molecules. CONCLUSION: The results not only provide a theoretical basis for the stability of plant protein emulsion systems, but also provide technical support for the production and processing of large-molecule plant proteins into emulsions in this field for improving their stability, and also provide more possibilities for other types of emulsions. © 2023 Society of Chemical Industry.

Emulsifying properties of O/W emulsion stabilized by soy protein isolate and γ-polyglutamic acid electrostatic complex.

In order to improve the emulsifying properties of soy protein around isoelectric point, soy protein isolate (SPI) and γ-polyglutamic acid (γ-PGA) complexes were prepared by electrostatic interaction. The formation of SPI-γ-PGA electrostatic complex and emulsifying properties were investigated by monitoring turbidity, zeta potential, intrinsic fluorophores, emulsion characterization, and microstructure observation. The results showed that the formation of SPI-γ-PGA electrostatic complex was identified through turbidimetric analysis and zeta-potential measurement. Intrinsic fluorescence spectrum indicated internal structure changes of electrostatic complexes. Furthermore, SPI-γ-PGA complex-stabilized emulsions showed better stability with small droplet sizes and slow growth as well as the uniform microstructure around the isoelectric point (pH 4.0-5.0) than SPI-formed emulsions. Under the different thermal treatments and ionic strengths, emulsions stabilized by SPI-γ-PGA-soluble complex resulted in improved emulsion stability to environmental stresses. This may be attributed to the increased steric repulsion and electrostatic repulsion by SPI-γ-PGA complexes at oil-water interfaces. The findings derived from this research would provide theoretical reference about SPI-γ-PGA electrostatic complex that can be applied in acid beverages and developed a novel plant-based sustainable stabilizer for emulsions. PRACTICAL APPLICATION: The electrostatic interaction between SPI and γ-PGA improved the emulsifying characteristics of soy protein around isoelectric point. The results derived from this research would expand applications of SPI-γ-PGA-soluble electrostatic complex that can be applied in acid beverages, as well as a novel plant-based sustainable stabilizer for emulsions.

Effect of emulsifiers on the properties of corn starch films incorporated with Zanthoxylum bungeanum essential oil.

The use of natural and safe ingredients in green food packaging material is a hot research topic. This study investigated the effect of different emulsifiers on starch film properties. Three types of emulsifiers, including Tween 80 as a small-molecule surfactant, sodium caseinate (CAS), whey protein isolate (WPI), and gelatin (GE) as macromolecule emulsifiers, whey protein isolate fibril (WPIF) as a particle emulsifier, were utilized to prepare Zanthoxylum bungeanum essential oil (ZBO) emulsions. The mechanical, physical, thermal, antibacterial properties, microstructure and essential oil release of starch films were investigated. CAS-ZBO nanoemulsion exhibited the smallest particle size of 198.6 ± 2.2 nm. The film properties changed with different emulsifiers. CAS-ZBO film showed the highest tensile strength value. CAS-ZBO and WPIF-ZBO films exhibited lower water vapor permeability than Tween-ZBO. CAS-ZBO film showed good dispersion of essential oil, the slowest release rate of essential oils in all food simulants, and the best antibacterial effect against Staphylococcus aureus and Listeria monocytogenes. The films composed of CAS-ZBO nanoemulsion, corn starch, and glycerol are considered more suitable for food packaging. This work indicated that natural macromolecule emulsifiers of CAS and WPIF are expected to be used in green food packaging material to offer better film properties.

Extraction of pectins from renewable grapefruit (Citrus paradisi) peels using deep eutectic solvents and analysis of their structural and physicochemical properties.

This study presents an innovative attempt to extract high-quality pectins from grapefruit (Citrus paradisi) peels by using deep eutectic solvents (DESs) as extraction agents. The maximum yield of betaine-citric acid (BC)-extracted pectin (BC-P) reached 36.47 % under the optimum process conditions: an L/S ratio of 25 mL/g, a pH of 2.0, and a temperature of 85 °C for 120 min. The yield of BC-P was significantly higher than HCl-extracted pectin (HCl-P, 8.76 %) under a pH of 2.0. In addition, the structural, physicochemical, and emulsifying properties of the purified pectins (BC-P and HCl-P) and commercial pectin (CP) were comparatively analyzed. Results showed that BC-P exhibited higher RG-I value, more arabinan side-chains, bigger Mw and Mn value than HCl-P. Moreover, the viscosity, G' and G'' of BC-P were significantly higher than those of HCl-P and CP. More importantly, BC-P demonstrated better emulsifying activity and stability compared to HCl-P and CP. When the concentration of BC-P was increased to 1.50 %, a stable emulsion containing a 50 % soybean oil fraction could be obtained. Our results confirmed that DESs can be considered as high-effective agents for pectin extraction. Pectins extracted from grapefruit peels can be as a promising natural emulsifiers that can be used in the food industry.

Bio-based Pickering emulsifier from mangosteen residues-derived sodium caseinate grafted spherical cellulose nanocrystals: Stability, rheological properties and microstructure studies.

This study focuses on the preparation of mangosteen rind-derived nanocellulose via green ascorbic acid hydrolysis. Subsequently, milk protein-grafted nanocellulose particles were developed as a renewable Pickering emulsifier for water-oil stabilization. The stabilizing efficiency of modified nanocellulose (NC-S) at different caseinate (milk protein) concentrations (1.5, 3.0, and 4.0 % w/v) was tested in a water-in-oil emulsion (W/O ratio of 40:60). At a concentration 3.0 % w/v of caseinate (3.0NC-S), the emulsion exhibited a stronger network of adsorption between water, Pickering emulsifier, and oil. This resulted in reduced oil droplet flocculation, increased stability over a longer period, and favorable emulsifying properties, as depicted in the creaming index profile, oil droplet distribution, and rheology analysis. Since 3.0NC-S demonstrated the best colloidal stability, further focus will be placed on its microstructural properties, comparing them with those of mangosteen rind (MG), cellulose, and nanocellulose (NC-L). The XRD profile indicated that both NC-L and NC-S possessed a cellulose nanocrystal structure characterized as type I beta with a high crystallinity index above 60 %. Morphology investigation shown that the NC-L present in the spherical shape of particles with nanosized ranging at diameters of 11.27 ± 0.50 nm and length 11.76 ± 0.46 nm, while modified NC-S showed increase sized at 14.26 ± 4.60 nm and length 14.96 ± 4.94 nm. The increment of particle sizes from NC-L to NC-S indicated 2.82 × 10-15 mg/m2 of surface protein coverage by caseinate functional groups.

Emulsion stability of hydroxybutyl chitosan as emulsifier at low pH: Effects of the degree of substitutions of hydroxybutyl groups.

Keeping the stability of emulsions at low pH is necessary for their successful applications in food and delivery systems. To achieve this goal, hydroxybutyl chitosan (HBC) with three degrees of substitution (DSs) was used as an emulsifier to investigate the effect of HBC structure on the emulsion stability. The DSs of HBC-5, HBC-10, and HBC-20 were 0.66, 1.51, and 2.19, respectively. The stability of oil-in-water emulsions against creaming/coalescence was positively correlated with the DS. As pH decreased to 2, HBC-20-stabilized emulsions were most stable without creaming or coalescence. After 30 days of storage, no changes in the droplet sizes of HBC-20-stabilized emulsions were observed, whereas the droplet sizes of HBC-5/10- stabilized emulsions significantly increased at low pH. The stability of HBC-20- stabilized emulsions at low pH was attributed to the higher surface activity and electrostatic repulsion. Our research revealed that the emulsion stability of HBC under low pH conditions can be controlled by the density of the hydroxybutyl groups in HBC. In vitro digestion further revealed the excellent stability of HBC-20-stabilized emulsions in simulated gastric fluid, which highlighted the enormous potential of HBC-20 to protect liposoluble drugs and nutrients from the extreme pH environment.