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Article

Study on the Synergistic Effect and Mechanism of Octenyl Succinic Anhydride-Modified Starch on the Stability of Myofibrillar Protein Emulsion

by
Peipei Yin
†,
Xiaozhong Bi
†,
Yuyu Xu
,
Tianhao Zhu
,
Qing Yin
,
Qingling Wang
and
Mangang Wu
*
College of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China
*
Author to whom correspondence should be addressed.
†
These authors contributed equally to this work.
Chemistry 2025, 7(4), 113; https://doi.org/10.3390/chemistry7040113
Submission received: 28 May 2025 / Revised: 3 July 2025 / Accepted: 10 July 2025 / Published: 16 July 2025
(This article belongs to the Section Food Science)
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Abstract

The effects of octenyl succinic anhydride-modified hydrophobic starch (OSA starch) on the properties of myofibrillar protein (MP) emulsions were investigated. The results show that the stability of protein emulsions was significantly enhanced with the addition of OSA starch (0.25–1.0%), with the most pronounced effect observed at a 1% concentration. Concomitantly, increasing OSA starch concentrations led to a reduction in the fat globule size. Electrostatic interactions between anionic groups in the modified starch and myofibrillar proteins were observed, which effectively decreased the zeta potential of the emulsion to a minimum of −52.3 mV. However, in the composite emulsion system, a competitive relationship between OSA starch and myofibrillar proteins was evident, as reflected by the decrease in interfacial protein content from 1.16 mg/mL in the control (CK) group to 0.78 mg/mL in the OSA starch-treated group. Despite this competition, the overall emulsion stability was improved due to the synergistic effects of the modified starch and proteins. These findings suggest that OSA-modified starch holds promise as a stabilizer for enhancing the stability of myofibrillar protein emulsions.

Graphical Abstract

1. Introduction

The emulsion is a dispersion system comprising two immiscible fluids under the action of an emulsifier, in which one phase is uniformly dispersed as smaller droplets within the other, forming a relatively stable emulsified system [1]. In emulsified food systems, proteins act as macromolecular surfactants, constructing a spatial network structure maintained by peptide bonds and intermolecular forces. This structure contains both hydrophilic and lipophilic groups, which effectively reduce interfacial tension between the two phases, thereby sustaining emulsion stability [2]. During emulsion homogenization, proteins spontaneously adsorb at the oil–water interface to form a dense protein film. This film effectively prevents droplet aggregation and ensures uniform emulsion dispersion [3]. Similarly, in meat composite gel products, fat distribution and stability also rely on protein function. Classical minced meat theory clarifies that protein membranes tightly encapsulate oil droplets to prevent aggregation, achieving complete fat emulsification [4]. Emulsified meat products can be viewed as specialized emulsion gel systems, with origins traceable to protein emulsions [5]. Proteins are natural polymeric emulsifiers with low dosage requirements and high emulsifying activity. However, protein emulsifiers have inherent flaws. The oil–water interface film they form is thin and is easily affected by factors such as temperature, ionic strength, and pH [6]. These defects often lead to problems such as fat precipitation and texture deterioration in emulsified meat products during production and storage. Therefore, it is necessary to conduct in-depth research on the properties of protein milk to provide theoretical support for the development of meat products.
The synergistic effect between solid particles and proteins has become a research focus. For example, Reger et al. elucidated the mechanism of clay particles and proteins collaborating to stabilize emulsions [7]. They found that the clay particles work collaboratively with the protein film on the surface of the oil droplets to create a three-dimensional network structure that provides the emulsion with extremely high stability. However, in the field of food production and processing, the research on the effect of edible solid particles on protein milk is still insufficient. The emulsion stabilized by small solid particles is called Pickering emulsion, which has significant advantages such as relatively small particle size distribution, high stability, low toxicity, and superior anti-coalescence properties [8]. Although particle stabilizers have been widely used in the preparation of Pickering emulsions, such as silica, alumina, wax, chitin, clay particles, titanium oxide, etc. [8,9,10]. Most of these studies have not directly involved the application in the food field [11]. In recent years, some potential food-compatible particle stabilizers have attracted attention and have been successfully applied in O/W Pickering emulsions, such as chitin nanocrystals [12], cellulose nanocrystals [13], and fat crystals [14], and their applications in the food field include ice cream, food preservation, and confectionery products, etc. It can improve the stability of the product and improve the taste of the product. It is worth mentioning that recent studies have also shown that hydrophobic modified raw starch can be used as a particle stabilizer to effectively stabilize O/W-type Pickering emulsions [15].
Plant-derived starch particles are abundantly available, cost-effective, renewable, and non-toxic, making them widely used in food processing. However, their natural hydrophilicity limits adsorption capacity during emulsification, a shortcoming addressable via octenyl succinic anhydride (OSA) modification to enhance hydrophobicity [16]. The modified starch, which contains the -COO group, is suitable for stabilizing O/W Pickering emulsions, exhibits significant surface activity [17], and can change water viscosity and stabilize oil-in-water emulsions. Its structure prevents droplets from flocculating and forms a dense film to prevent emulsion accumulation [18]. This starch also performs well at low concentrations and is non-toxic, biodegradable, and suitable for industrial production; so, it is widely used in various emulsion products. In addition, OSA-modified starch (OSAS)-stabilized Pickering emulsion can also improve the gel properties of myofibrillar protein (MP). Wang et al. used OSAS of different crystal types to stabilize a Pickering emulsion as a novel MP gel particle filler and studied its effect on gel properties. The results showed that the storage modulus, gel strength, and water holding capacity of the OSAS-stabilized meat protein gel filled with the Pickering emulsion were better than those of the pure MP gel [19]. Mi et al. studied the effects of different modified starches on surimi protein gel, and the results showed that the addition of modified starch improved the water retention and gel strength of surimi gel and made the gel structure more compact [20]. These results indicate that hydrophobic modified starch is an effective modifier that can significantly improve the performance of meat protein gels. However, these studies have only focused on gel modification. Whether and how OSAS can directly enhance the stability of the emulsification system of meat proteins (such as MP), and what the molecular interaction mode of OSAS and MP at the oil–water interface is remain unknown at present. The absence of this key mechanism has greatly hindered the precise application of OSAS in emulsified meat products.
The primary objective of this study was to investigate the effects of octenyl succinic anhydride (OSA)-modified starch on the emulsification stability of myofibrillar proteins. Furthermore, the specific mechanisms of hydrophobically modified starch at varying concentrations (0.25%, 0.5%, 0.75%, and 1%) on protein emulsion properties were elucidated. The results reveal the role of hydrophobically modified starch in enhancing myofibrillar protein emulsification stability, providing a theoretical foundation for developing low-fat emulsified minced meat products.

2. Materials and Methods

2.1. Materials

About 10 kilograms of fresh pork tenderloin muscle, with a pH level ranging from 5.6 to 5.9, was procured from Yangzhou Xiangtai Meat Trading Center (24–48 h post-mortem). Next, the samples were deboned, and the visible external fat was trimmed. The lean tissue was then cut into cubes of approximately 1 cm3, mixed, and divided into 60 g portions. Finally, these portions were placed in plastic vacuum package bags, which were subsequently evacuated and stored at −80 °C until use.
Native rice starch was acquired from Shanghai Senghang Food Co., Ltd. (Shanghai, China). Sunflower seed oil was purchased from a local market. Octenyl succinic anhydride (OSA) was supplied by Nanjing Gutian Biochemical Co., Ltd. (Nanjing, China). All chemicals of analytical grade were obtained from Sinopharm Chemical Reagent Co., Ltd. (Shanghai, China) and Sangon Biotech Co., Ltd. (Shanghai, China).

2.2. Preparation of Hydrophobic Starch Particles

Accurately weighed 20 g of rice starch was suspended in distilled water to acquire a concentration of 30% (w/w). After the pH of the starch suspension was adjusted to 8.5 with 3% NaOH, OSA, which had been diluted 5 times with isopropyl alcohol, was added dropwise to the continuously stirred suspension at a final concentration of 3% (w/w, dry starch basis) at 35 °C for 2 h. Following that, the reaction was permitted to continue for 3 h at 35 °C. Subsequently, the reaction was terminated by adjusting the pH to 7 using 3% HCl. After the reaction, the modified starch was recovered via centrifugation, preceded by a thorough washing process, which involved rinsing twice with distilled water and twice with ethanol. The resulting granules were dried at 45 °C for 24 h and subsequently passed through a 120-mesh sieve (125 mm opening) to prepare them for further utilization [21].

2.3. Determination of Degree of Substitution (DS) of Hydrophobically Modified Starch

The DS of OSA-modified starch was ascertained through the utilization of a titration method [22]. The modified starch sample, weighing 2.5 g on a dry basis, was uniformly dispersed in 25 mL of distilled water. Subsequently, 25 mL of 0.5 M NaOH solution was added to the mixture. After allowing the reaction to proceed at 25 °C for 24 h, excess alkali present was titrated with 0.5 M HCl, utilizing phenolphthalein as the titration indicator. The native starch underwent the same treatment conditions and served as a reference. The DS was calculated based on the OSA substitution value. The DS is calculated as follows:
D S = 162.4 A 1000 − 210 A
A = C V W
where 162.4 is the molar mass of glucose residue, g/mol; 210 is the molar mass of octenyl succinic anhydride, g/mol; A is the mass of NaOH consumed, mmol/g; V is the volume of NaOH consumed, mL; C is the molar concentration of NaOH, mol/L; and W is the mass of the sample, g.

2.4. Determination of Hydrophobic Modified Starch by Fourier Transform Infrared Spectroscopy (FTIR)

A Cary 610/670 micro-infrared spectrometer (Agilent Technologies, Santa Clara, CA, USA) was used for FTIR analysis to reflect changes in the chemical structure of starch samples. During the experiment, natural starch and OSA starch granules were mixed with potassium bromide (KBr) powder at a certain ratio (1:100, w/w), and tablets were prepared by the tablet-pressing mechanism for determination. Each sample was scanned 32 times at a resolution of 4 cm−1, with the wave number range set from 400 to 4000 cm−1 [23].

2.5. Preparation of MP

MP was extracted from pork muscle samples thawed at 2–4 °C using an isolation buffer consisting of 0.1 M NaCl, 10 mM sodium phosphate, 2 mM MgCl2, and 1 mM EGTA at pH 7.0. The isolated MP pellets were washed twice via suspension in four volumes of 0.1 M NaCl. The pH of the suspension was adjusted to 6.2, and the resulting mixture was centrifuged at 2000× g. The purified MP pellet was stored on crushed ice and utilized within 2 days of isolation [24]. The concentration of protein was determined using the traditional Biuret method, with bovine serum albumin (Sinopharm Chemical Reagent Co., Ltd., Shanghai, China) serving as the standard.

2.6. Preparation of Emulsions

Oil-in-water emulsions were prepared with sunflower seed oil and 1% MP solution (0.6 M NaCl, 50 mM sodium phosphate, pH 6.2). A total of 2 g of sunflower seed oil was added to 8 g of an MP solution. Dried different concentrations of OSA starch granules (0.25%, 0.5%, 0.75%, and 1%) and 1% Tween 80 were dispersed in the prepared emulsions, and 1% MP was used as CK (control check). The Ultra-Turrax homogenizer (IKA T18, IKA-Werke GmbH & Co. KG, Staufen, Germany) was then used for homogenization at 12,000 rpm with 40 s intervals at room temperature [25].

2.7. Emulsifying Properties

The emulsifying activity index (EAI) and the emulsion stability index (ESI) were determined according to the method of [26,27] with slight modifications. For the EAI and ESI measurements, the volume of 20 μL of freshly prepared emulsions were taken from the bottom of the homogenized emulsions exactly 0 min, 10 min, 30 min, 60 min, and 120 min after homogenization and diluted with 5 mL of 0.1% (w/v) SDS. The absorbance of the emulsion at 500 nm was immediately measured. The EAI and ESI values were calculated as follows:
E A I   m 2 / g = 4.606 × A 0 C × ( 1 − φ ) × 10 4 × N
E S I   ( % ) = A t A 0 × 100
where A0 and At represent the absorbance of the emulsions taken at 0 min and 10, 30, 60, and 120 min; C is the protein concentration (g/mL) before emulsification; φ indicates the oil volume fraction (v/v) of the emulsion; and N is the dilution factor (251).

2.8. Viscosity of Emulsions

The apparent viscosity of the emulsion was determined by flow measurement using the shear rate method at 25 °C. The KINEXUS Pro rheometer (Malvern Instrument, Inc., Worcestershire, UK), equipped with the PU40 probe, was used while choosing the cone–plate geometry. In order to ensure the accuracy and reliability of the measurement results, the sampling parameters were set to the shear rate range of 0.01–1 s−1 and the pitch of 1.0 mm [28].

2.9. Determination of the Particle Size and Particle Size Distribution

Malvern MasterSizer 3000 (Malvern, Worcestershire, UK) is based on the principle of laser light source and scattering measurement. This experiment is used to measure the mean diameter and particle size distribution of oil droplets in emulsions at room temperature. The analysis mode was as follows: HydroLV was used as the injector, the particle refractive index was 1.520, and the particle absorption rate was 0.1. Water was selected as the dispersant, and its refractive index was 1.330. The sensor threshold was set to 100, the background test duration was set to 15 s, and the stirring speed was set to 2000 r/min. D(x) 10, D(x) 50, and D(x) 90 represent the percentiles of effective diameter size (EDS) of oil droplets, corresponding to positions of 10%, 50% (median), and 90% in the cumulative particle size distribution, respectively [29].

2.10. Zeta Potential Measurements

The zeta potential of various fresh emulsions was measured at room temperature with a ZetaSizer Nano-ZS instrument (Malvern Instruments Co. Ltd., Worcestershire, UK). To ensure accuracy and reproducibility, each measurement was repeated three times [30].

2.11. Determination of Thiol Content in Emulsion

The content of sulfhydryl groups was determined by Ellman’s 5,5′-dithiobis -(2-nitrobenzoic acid) (DTNB) method [31]. Take 3 mL of sample solution, add 3 mL of 0.1 M phosphate buffer containing EDTA and 1% SDS, then add 0.1 mL of DTNB, and after vortex mixing, incubate in a water bath at 25 °C for 1 h, and then centrifuge at 10,000× g for 30 min. At the same time, the DTNB group was used as the control group. The supernatant was taken at 412 nm to measure the absorbance, and the extinction coefficient was calculated as 13,600 M−1 cm−1.

2.12. Determination of Interfacial Protein Content

The prepared protein emulsion was centrifuged at 12,000× g for 10 min at a temperature of 4 °C. After centrifugation, the liquid under the centrifuge tube was transferred by syringe and filtered by a filter membrane. The protein content was determined by the Biuret method.

2.13. Statistical Analysis

This study used a randomized block design, repeated measurements, and all experiments were repeated at least 3 times (n = 3). The SPSS (13.0) software (SPSS, Chicago, IL, USA) was used for statistical analysis. The data were analyzed by a one-way ANOVA. LSD test was used for the difference of the mean of each treatment, and p < 0.05 was considered significant.

3. Results

3.1. Hydrophobic Modified Starch Substitution Degree

The degree of substitution of hydrophobic modified starch was 0.019. The World Health Organization (WHO) and the United States Food and Drug Administration (FDA) have formulated the addition and quality standards of octenyl succinate starch ester: when used as a food additive, its degree of substitution shall not exceed 0.02; at the same time, the additive amount of octenyl succinate anhydride used is generally not more than 3%. The hydrophobic modified starch obtained in this experiment conforms to these standards; so, it can be applied in foods [32].

3.2. Fourier Transform Infrared Spectroscopy (FTIR)

The infrared spectra of natural starch and hydrophobic modified starch are shown in Figure 1A and 1B, respectively. Both kinds of starches showed characteristic peaks of different functional groups at specific wave numbers in the IR spectra. A large peak corresponding to the hydroxyl group appeared near 3382 cm−1, and the C-H stretching vibration peak of the starch molecule appeared near 2932 cm−1 [33]. The strong absorption peaks at 1648 cm−1, 1418 cm−1, and 1350 cm−1 are C-O stretching vibration peaks of starch molecules [33]. In particular, the absorption peak near 1645 cm−1 may be due to the water molecules within the starch molecules bound by the aqueous environment. However, in Figure 1B, new absorption peaks appeared at 1242 cm−1 and 1222 cm−1, which were carbonyl stretching vibration peaks of modified starch molecules, indicating that the esterification of octenyl succinic anhydride and starch was successfully completed.

3.3. Emulsifying Properties

The increase in the emulsifying activity index (EAI) and emulsion stability index (ESI) can be characterized to the formation and stabilization of the emulsion. It can be seen from Figure 2 that the synergistic effect of modified starch granules or Tween 80 will significantly improve the emulsification activity of the composite protein emulsion (p < 0.05), while the modified starch granules are better than Tween 80 [34]. When the concentration of OSAS particles was 1%, the EAI of the protein emulsion was the highest. The modified starch particles showed a synergistic effect with the oil phase or protein in the emulsion, enhancing the ability of oil particles or oil droplets to adsorb protein on its surface. This increased protein adsorption leads to increased protein mass and promotes the formation of protein film on the surface of particles or oil droplets, so that particles or oil droplets cannot be close to each other, thus enhancing the stability of the protein emulsion system [35]. In a food emulsion system, the EAI of a protein-stable emulsion is generally determined by the properties of the protein adsorption layer on the surface of the droplet. Adding an appropriate amount of modified starch particles not only helps to increase the density of the protein adsorption layer and enhance its structure, but also effectively reduces the aggregation between droplets and improves the stability of the emulsion [36].
Table 1 shows the effects of Tween 80 and different concentrations of modified starch particles on the emulsification stability of protein emulsion. As shown in Table 1, the addition of emulsifier has the same effect on the emulsification stability of protein emulsions, and the trend is that it first increases with the increase in the placement time, and then gradually decreases, and the stability is always higher than that of the CK (control) emulsion group. However, at the same time, the modified starch particles have the most significant effect on improving the ESI of protein emulsion; this result follows the trend shown in Figure 3. In addition, the ESI of the protein emulsion will gradually decrease with the passing of time, which shows the highest stability at 10 min and decreases to the lowest value after 120 min. There may be many reasons for this change in stability. Firstly, as the content of modified starch particles increases, the viscosity of the protein emulsion system increases, and the modified starch particles may form a weak gel structure in the protein network, effectively limiting the aggregation of fat particles and thus improving the stability of the emulsion [37]. However, as time passes, the number of emulsified denatured starch particles in the system decreases, and these unabsorbed particles may lead to flocculation through bridging or repulsion, thus destroying the stability of the emulsion [38]. In addition, the increase in the content of modified starch particles may also cause changes in the osmotic pressure of the system, narrowing the distance between fat particles and triggering aggregation [39], which is also one of the reasons for the decline in the stability of the emulsion.

3.4. Emulsion Apparent Viscosity

The influence of Tween 80 and different concentrations of modified starch particles on the apparent viscosity of protein emulsion is shown in Figure 3, from which the protein emulsion stabilized by Tween 80 or different concentrations of OSA starch presents obvious differences in viscosity (p < 0.05). At a lower shear rate, the apparent viscosity decreases sharply with the increase in the shear rate, that is, the fluid has a shear thinning phenomenon [40]. Conversely, at a higher shear rate, the decrease in viscosity becomes smaller and the degree of shear thinning decreases with the increase in the shear rate, which may be due to the gradual consistency of protein molecule movement direction, the decrease in intermolecular friction resistance, the break of chemical bonds such as hydrogen bonds, and finally the dissociation of protein molecules [41,42]. At a lower shear rate, the viscosity of the emulsion decreases sharply with the increase in the shear rate. When the shear rate reaches a high level, the viscosity of the emulsion decreases very little. The main reason for this phenomenon may be that, under the action of shearing stress, the orientation of the droplet is significant, and its effect is much higher than the random effect caused by Brownian motion, resulting in a rapid decrease in viscosity. However, when the shear force reaches a certain degree, the droplets tend to be oriented, and the apparent viscosity of the emulsion tends to be stable and no longer decreases significantly [43]. When the concentration of modified starch particles was 1%, the apparent viscosity of myofibrillar protein emulsion increased from 99.8 to 417.6 Pa.s, which may be due to the thickening effect of modified starch. The high concentration of modified starch particles, due to the strong hydrophobic interaction between the particles, is conducive to the formation of an enhanced interconnected network structure, which significantly improves the viscosity of the emulsion system. At the same time, the high apparent viscosity can effectively prevent the free movement of oil droplets under the action of gravity or Brownian motion, and then inhibit the fusion, aggregation, or sedimentation of oil droplets, and ultimately improve the stability of protein emulsion [44]. The results in Table 1 confirm this analysis.

3.5. Emulsion Particle Size Distribution

The emulsion fat granule size distribution of dispersed phase in the emulsion are the key factors affecting its physical and chemical properties. The granule size of food emulsions is widely distributed, showing typical polydispersity characteristics. The particle size distribution of multiphase emulsions, such as unimodal, bimodal, or multi-modal, mainly depends on the number of peaks in the particle size distribution [45,46]. Figure 4 shows the particle size distribution of modified starch particles and complex protein emulsions with different concentrations. The particle size distribution curve of the whole population presents a typical “bimodal” shape, and the bimodal range is different. Specifically, the first peak of the “twin peaks” is mainly in the range of 0.1~2.75 μm, and the second peak appears in the range of 7~500 μm. The trend of each group was the same, and the particle size distribution range was narrow, indicating that the smaller the particle dispersion degree, the higher the concentration. Compared with other groups, the droplet size distribution of the emulsion in the CK group was wider [47]. With the increase in the concentration of modified starch particles, the peak value of large droplets in the emulsion gradually moved to the left, while the peak value of small droplets remained stable in the lateral position, but the peak height increased. This change in particle size distribution helped to improve the stability of the emulsion. It is worth noting that, with the increase in the concentration of modified starch particles, the particle size and the proportion of particles to the total number of particles in each group gradually decreased, indicating that the particle distribution in the emulsion became more concentrated, which further enhanced the stability of the protein emulsion [48].
D(x) 10, D(x) 50, and D(x) 90 in Table 2 represent the particle size of the cumulative volume of the emulsion particles at 10%, 50%, and 90% of the total volume, respectively. It can be seen from the table that, with the increase in the concentration of modified starch particles, the emulsion granule sizes of D(x) 10, D(x) 50, and D(x) 90 in the emulsion are significantly reduced (p < 0.05). When 1% modified starch particles are added, the emulsion granule size is the smallest, which means that adding a certain amount of modified starch particles can better emulsify fat and reduce the aggregation between fat granules, thus reducing the granule size in the emulsion. The experimental results are consistent with those of Mcclements et al. It is generally believed that the smaller the emulsion fat granule size, the better the stability [49]. Therefore, we can infer that the granule size of the emulsion may be determined by the concentration of modified starch particles when other conditions in the CK emulsion system are constant. The main reason may be due to the synergistic interaction between the particulate emulsifier and the myofibrillar protein in the emulsion system, which can solve the influence of poor stability of the single emulsifier to some extent [50]. The granule size of the emulsion decreased significantly with the addition of modified starch particles (p < 0.05); the ESI of the protein emulsion was significantly improved, as shown in Table 1. The possible reason is that the increased concentration of modified starch particles promotes the faster adsorption of myofibrillar protein to the interface and reduces the interfacial tension, thereby reducing the emulsion granule size of the oil droplets. Therefore, the addition of the modified starch particle emulsifier and protein can effectively reduce the number of large droplets and improve the stability of the emulsion system through a synergistic effect.

3.6. Emulsion Potential

The interface charge density of the emulsion system can reflect the electrostatic interaction between the systems, thus affecting the stability of the emulsion. By monitoring the potential of the emulsion system, it is helpful to judge the relative stability of the emulsion system [47,50]. The higher absolute value of the potential indicates that the emulsified droplets tend to be stable, the repulsive force between the small droplets is greater than the attractive force, and the dispersion system is stable without condensation. The lower potential values indicate that the electrostatic repulsion between the emulsified droplets is not sufficient to resist the various attractive forces between the systems, resulting in the destruction of the dispersion, the flocculation of the droplets, and the stability of the final product [51].
As shown in Figure 5, with the increase in the amount of modified starch particles, the potential (absolute value) of the composite emulsion gradually increased. The absolute value of the potential in all treatment groups was significantly higher than that in the CK (control) group (p < 0.05), and the effect of modified starch particles was higher than that of Tween 80 emulsifier, indicating that the addition of OSA-modified starch had a significant effect on the potential of protein emulsion. The results follow the trend shown in Figure 1. When the concentration of modified starch was 1%, the lowest potential value was −52.3 mV. The main reason may be that the starch molecule modified by octenyl succinic anhydride has a negative charge group, while OSA-modified starch belongs to anionic starch [52]. Therefore, the modified starch particles and myofibrillar protein molecules bind to each other through hydrophobic interaction or hydrogen bonding, resulting in a change in the conformation of myofibrillar protein emulsion, exposing its negative electric groups, and increasing its surface charge density. Then, the negatively charged groups interact with the negatively charged groups on the modified starch particles to reduce the electric potential of the system. At the same time, the interaction between groups helps to reduce the attraction and aggregation between water droplets, enhance the stability of the oil–water interface, and improve the stability of the emulsion system.

3.7. Emulsion Thiol Content

Figure 6 shows the effect of different concentrations of modified starch particles and the effect of Tween 80 on the sulfhydryl content of myofibrillar protein emulsion. It can be seen from the figure that the two emulsifiers are significantly lower than the CK group (p < 0.05). The content of myofibrillar protein emulsion sulfhydryl group decreased significantly (p < 0.05). Similarly, the emulsion after adding modified starch particles exhibited a more pronounced decrease (p < 0.05). When the concentration of modified starch particles was 1%, the content of myofibrillar protein emulsion sulfhydryl group was the lowest. This trend reverses previous trends. The reduced content of thiol can indicate the enhanced interaction between the modified starch particles and the protein in the protein emulsion [53]. When the modified starch interacts with the protein, it will directly or indirectly act on the head of the myofibrillar protein. Most of the sulfhydryl groups in myofibrillar proteins are embedded in the molecular head, which changes the spatial structure of myofibrillar proteins. At the same time, studies have also found that the polysaccharide content has an effect on the total sulfhydryl content of myofibrillar protein [54]. The addition of polysaccharides and other substances leads to the unfolding of the myofibrillar protein structure, which facilitates the transformation between the thiol-based contacts, resulting in a decrease in sulfhydryl content. The decrease in the sulfhydryl content indicates that, in the protein composite emulsification system, the OSA-modified starch granules can enhance the cross-linking with proteins by acting on the myofibrillar protein head and protein.

3.8. Content of Interfacial Protein in Composite Protein Emulsion

The protein in the emulsion system can be rapidly adsorbed to the surface of the fat granules during the emulsion homogenization process, forming a viscoelastic interfacial film to block the direct contact between the fat granules and effectively prevent the aggregation of the fat granules, thus ensuring that the stable state of the emulsion system can be maintained. It is worth noting that the concentration of protein at the interface plays an important role in the emulsion particle size distribution and overall stability of the emulsion [55]. As shown in Figure 7, the interfacial protein content of the CK (control MP group) was 1.16 mg/mL without adding any other stabilizer. However, the content of the interfacial protein in the emulsion showed a decreasing trend when the stabilizer was added. Particularly, after the addition of 1% OSA-modified starch, the content of interfacial protein dropped to the lowest value of 0.78 mg/mL, which indicates that there is an obvious competitive adsorption between proteins and other emulsifiers [56]. The decrease in the content of interfacial protein is probably due to the fact that the modified starch particles act as the emulsifier to form a Pickering emulsion at this time, and thus produce a certain competitive adsorption effect with the protein. The addition of OSA starch particles to the protein emulsion not only increases the viscosity of the system, but also slows down the process of protein adsorption and development. At the same time, competitive adsorption with proteins also occurs, which affects the distribution of proteins in fat granules films and may reduce the protein content at specific locations (such as the surface of the emulsion drop). This competitive adsorption aligns with findings in emulsion-filled protein gels, where the interfacial composition directly influences mechanical properties and microstructure by altering the protein distribution at the interfaces [57]. In our system, OSA starch may similarly dominate the interface, reducing the protein coverage but enhancing stability through particle jamming.

4. Discussion

This study systematically analyzed the effects of different concentrations of OSA modified starch on the performance of myofibril emulsions, revealing its key role and potential mechanism in improving the stability of emulsions. The experimental results demonstrate that the incorporation of OSA-modified starch (0.25–1.0%) significantly enhanced both the emulsifying activity index (EAI) and the stability index (ESI) of the emulsion, with the optimal performance observed at a concentration of 1% (as shown in Figure 2). This phenomenon was likely attributable to the hydrophobic modification characteristics of OSA starch. The octenyl succinate group (-COO) introduced into the OSA starch molecule imparted amphiphilic properties, enabling it to adsorb at the oil–water interface and form a compact particle film, thereby reducing interfacial tension and preventing droplet coalescence. Furthermore, the synergistic interaction between OSA starch and myofibrillar proteins strengthened the mechanical integrity of the interfacial membrane via hydrophobic interactions or hydrogen bonding. With the increase in the OSA starch concentration, there was a significant decrease in the size of fat globules (D(x) 10, D(x) 50, and D(x) 90) in the emulsion (Table 2). This suggests that starch particles competitively adsorbed onto the droplet surfaces, thereby replacing some proteins and forming smaller, more uniformly distributed droplets. Smaller droplet sizes could effectively mitigate aggregation caused by gravitational sedimentation and Brownian motion, thus enhancing the overall stability of the emulsion. Additionally, the bimodal characteristics of particle size distribution (Figure 4) might indicate the dynamic equilibrium of interfacial adsorption between starch particles and proteins. At low concentrations, proteins predominantly dominated the adsorption process, whereas at higher concentrations, starch particles occupied more interfacial sites, forming a tighter physical barrier that contributed to improved emulsion stability. After adding OSA starch, the absolute value of the Zeta potential of the emulsion increased significantly (Figure 5), reaching up to 52.3 mV at the highest. This phenomenon was attributed to the electrostatic repulsion between the anionic groups of OSA starch and the negative charges on the surface of myofibrils, which weakened the van der Waals attraction between droplets and thereby inhibited aggregation. The experiment found that the content of thiol (-SH) in the emulsion significantly decreased after adding the OSA starch (Figure 6), suggesting that cross-linking occurred between starch and protein molecules, resulting in the conformational expansion of myofibrils and the exposure of the internal hydrophobic groups. This process might promote the formation of a denser interfacial film by enhancing the interfacial adsorption capacity of proteins. The addition of 1% OSA starch reduced the interfacial protein content from 1.16 mg/mL (CK group) to 0.78 mg/mL (Figure 7), indicating that there was competitive adsorption between starch particles and proteins at the oil–water interface. Due to its higher surface activity and hydrophobicity, OSA starch might preferentially occupy the interface sites and form a stable layer mainly composed of particles. Although the reduction in interface proteins might weaken the continuity of protein membranes, the physical barrier effect of starch particles compensated for this defect, indicating that, in a complex emulsification system, the synergistic effect between particles and proteins was crucial for stability.

5. Conclusions

This study systematically investigates the effects of hydrophobic modified starch particles on the properties of myofibrillar protein emulsions. The results demonstrate that incorporating modified starch particles significantly enhances emulsion stability and emulsification activity, elevates initial viscosity, mitigates droplet aggregation, and strengthens system stability. OSA-modified starch particles interact with the protein emulsion to increase the population of small droplets, further stabilizing the system. Anionic groups within the starch exhibit electrostatic interactions with myofibrillar proteins, reducing the zeta potential. Additionally, modified starch particles act on the protein molecular heads to form aggregates, decreasing the sulfhydryl group content and influencing emulsification characteristics. Notably, modified starch particles compete with protein molecules for interfacial adsorption, preferentially accumulating at the oil–water interface and reducing interfacial protein content. This reveals that OSA starch dominates the emulsion stabilization mechanism via competitive interface adsorption, challenging the traditional paradigm of protein-driven stabilization. These findings deepen our understanding of OSA-starch granules in protein stabilization and provide a theoretical foundation for their application in the food industry. Future research may explore higher starch concentrations or different modification degrees to optimize emulsification, holding potential for applications in high-pressure processed foods and 3D-printed meat substitutes.

Author Contributions

Conceptualization, M.W., P.Y. and X.B.; methodology, M.W., X.B. and P.Y.; data curation, T.Z., Q.Y., P.Y. and X.B.; writing—original draft preparation, P.Y. and Y.X.; writing—review and editing, all authors; formal analysis, all authors; visualization, M.W., X.B. and P.Y.; supervision, M.W.; project administration, M.W. and Q.W.; funding acquisition, M.W. and Q.W. All authors have read and agreed to the published version of the manuscript.

Funding

This research was funded by projects from National Natural Science Foundation of China (Grant No. 32272335, 32302110) and supported by Postgraduate Research & Practice Innovation Program of Jiangsu Province (SJCX24_2367), and Yangzhou University Student Science and Technology Innovation Fund (XCX20241113).

Data Availability Statement

The original contributions presented in the study are included in the article; further inquiries can be directed to the corresponding author.

Acknowledgments

Thanks to all the authors for checking and reviewing this article. Thanks to the funding from National Natural Science Foundation of China and Yangzhou University Student Science and Technology Innovation Fund.

Conflicts of Interest

The authors declare no conflicts of interest.

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Figure 1. Fourier transform infrared spectroscopy (FTIR) of natural starch (A) and hydrophobic modified starch (B).
Figure 1. Fourier transform infrared spectroscopy (FTIR) of natural starch (A) and hydrophobic modified starch (B).
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Figure 2. Changes in the emulsifying activity index of different hydrophobically modified starch granule concentration. Different letters indicate significant differences between means (p < 0.05).
Figure 2. Changes in the emulsifying activity index of different hydrophobically modified starch granule concentration. Different letters indicate significant differences between means (p < 0.05).
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Figure 3. Rheological curve of composite protein emulsion with different concentrations of hydrophobically modified starch granules.
Figure 3. Rheological curve of composite protein emulsion with different concentrations of hydrophobically modified starch granules.
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Figure 4. Effect of the hydrophobically modified starch particle concentration on the particle size distribution of the protein emulsion.
Figure 4. Effect of the hydrophobically modified starch particle concentration on the particle size distribution of the protein emulsion.
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Figure 5. Effect of hydrophobically modified starch particle concentration on the protein emulsion potential. Different letters indicate significant differences between means (p < 0.05).
Figure 5. Effect of hydrophobically modified starch particle concentration on the protein emulsion potential. Different letters indicate significant differences between means (p < 0.05).
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Figure 6. Effect of hydrophobically modified starch particle concentration on the content of sulfhydryl groups in the protein emulsion. Different letters indicate significant differences between means (p < 0.05).
Figure 6. Effect of hydrophobically modified starch particle concentration on the content of sulfhydryl groups in the protein emulsion. Different letters indicate significant differences between means (p < 0.05).
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Figure 7. Effect of the hydrophobically modified starch particle concentration on the interfacial protein content of the protein emulsion. Different letters indicate significant differences between means (p < 0.05).
Figure 7. Effect of the hydrophobically modified starch particle concentration on the interfacial protein content of the protein emulsion. Different letters indicate significant differences between means (p < 0.05).
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Table 1. The emulsifying stability index of different hydrophobically modified starch granule concentrations.
Table 1. The emulsifying stability index of different hydrophobically modified starch granule concentrations.
TreatmentTime
10 min30 min60 min120 min
CK (1% MP)0.292 ± 0.033 fA0.251 ± 0.010 fB0.232 ± 0.031 fC0.212 ± 0.041 fD
MP + 1% T800.313 ± 0.020 eA0.294 ± 0.023 eB0.262 ± 0.040 eC0.242 ± 0.053 eD
MP + 0.25% OSAS0.402 ± 0.031 dA0.358 ± 0.054 dB0.287 ± 0.070 dC0.253 ± 0.034 dD
MP + 0.5% OSAS0.511 ± 0.022 cA0.425 ± 0.043 cB0.398 ± 0.032 cC0.303 ± 0.050 cD
MP + 0.75% OSAS0.589 ± 0.063 bA0.503 ± 0.070 bB0.455 ± 0.040 bC0.351 ± 0.053 bD
MP + 1% OSAS0.612 ± 0.030 aA0.568 ± 0.030 aB0.503 ± 0.063 aC0.468 ± 0.070 aD
Note: The 1% T 80 represents that the concentration of Tween 80 is 1%, and 0.25%, 0.5%, 0.75%, 1.0% refer to different concentrations of OSA-modified starch solutions, and CK (Control Check) is the MP with a concentration of 1%. Different letters (a–f) indicate significant differences between means in the same column (p < 0.05). Different letters (A–D) indicate significant differences between means in the same row (p < 0.05).
Table 2. Effect of the hydrophobically modified starch particle concentration on the particle size of the protein emulsion.
Table 2. Effect of the hydrophobically modified starch particle concentration on the particle size of the protein emulsion.
TreatmentD(x) 10D(x) 50D(x) 90
CK (1% MP)0.575 ± 0.025 a26.354 ± 0.722 a77.453 ± 0.802 a
MP + 1% T 800.522 ± 0.009 b18.264 ± 0.912 b52.049 ± 0.800 b
MP + 0.25% OSAS0.486 ± 0.006 c12.657 ± 1.129 c36.214 ± 0.954 c
MP + 0.5% OSAS0.426 ± 0.007 d6.824 ± 0.125 d34.269 ± 0.764 c
MP + 0.75% OSAS0.398 ± 0.012 de1.569 ± 0.006 e31.069 ± 1.356 d
MP + 1% OSAS0.375 ± 0.004 e1.262 ± 0.004 e28.654 ± 0.695 e
Note: The 1% T 80 represents that the concentration of Tween 80 is 1%, and 0.25%, 0.5%, 0.75%, 1.0% refer to different concentrations of OSA-modified starch solutions, and CK is the MP with a concentration of 1%. Different letters indicate significant differences between means (p < 0.05).
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Yin, P.; Bi, X.; Xu, Y.; Zhu, T.; Yin, Q.; Wang, Q.; Wu, M. Study on the Synergistic Effect and Mechanism of Octenyl Succinic Anhydride-Modified Starch on the Stability of Myofibrillar Protein Emulsion. Chemistry 2025, 7, 113. https://doi.org/10.3390/chemistry7040113

AMA Style

Yin P, Bi X, Xu Y, Zhu T, Yin Q, Wang Q, Wu M. Study on the Synergistic Effect and Mechanism of Octenyl Succinic Anhydride-Modified Starch on the Stability of Myofibrillar Protein Emulsion. Chemistry. 2025; 7(4):113. https://doi.org/10.3390/chemistry7040113

Chicago/Turabian Style

Yin, Peipei, Xiaozhong Bi, Yuyu Xu, Tianhao Zhu, Qing Yin, Qingling Wang, and Mangang Wu. 2025. "Study on the Synergistic Effect and Mechanism of Octenyl Succinic Anhydride-Modified Starch on the Stability of Myofibrillar Protein Emulsion" Chemistry 7, no. 4: 113. https://doi.org/10.3390/chemistry7040113

APA Style

Yin, P., Bi, X., Xu, Y., Zhu, T., Yin, Q., Wang, Q., & Wu, M. (2025). Study on the Synergistic Effect and Mechanism of Octenyl Succinic Anhydride-Modified Starch on the Stability of Myofibrillar Protein Emulsion. Chemistry, 7(4), 113. https://doi.org/10.3390/chemistry7040113

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