Mung Bean Protein Isolate Research Articles

Investigating the role of starch in the structuring of meat alternatives from mung bean and pea protein isolates via heat-induced gelation

IntroductionThe structuring of plant-based meat alternatives is a complex process which is highly dependent on qualitative and quantitative proportion of different ingredients. In the present study, starch, protein, and oil concentrations were optimized for the formulation of meat alternative (MA) using response surface methodology (RSM).MethodsProtein isolates of mung bean and pea protein, & corn starch were used along with sunflower oil to formulate meat alternatives using heat-induced gelation. The protein functionality of mungbean protein isolate (MBPI) and pea protein isolate (PPI) were analyzed. In addition, the effects of constituent composition on the physicochemical properties of meat alternatives were studied using RSM.ResultsThe protein content exhibited an elevation with increased levels of MBPI and PPI in 15:15 ratio. Moisture and hardness were chiefly influenced by oil content, as they displayed a decline with increasing oil levels. The color (L*) was principally affected by starch and oil, where the L* reduced with increasing levels of both variables. Springiness was influenced by the interaction of protein ratio (MBPI:PPI) and starch, as it showed a lowest value at the lowest level of protein and the highest level of starch. Chewiness was influenced by the interaction of hardness and springiness. The microstructure analysis showed dense protein matrix in the meat alternative.DiscussionOverall, the study shows that starch facilitated the structuring of meat alternative formulated using MBPI and PPI which could be utilized as potential materials for enhanced textural properties of the meat alternatives.

Synergistic effects of alkaline and heat treatments on structural and functional properties of mung bean protein isolate: improving physicochemical stability of plant‐based emulsions

SummaryPlant‐based meat alternatives often require fat replacers to mimic the texture of traditional products. This study aimed to develop plant‐based emulsion gels using mung bean protein isolate (MBPI) as a potential fat substitute. However, creating these gels via heat setting requires a high protein concentration, which demands modification of the MBPI structure to enhance emulsifying properties. This study investigated synergistic effects of alkaline treatment (0.3 or 3.5% Na2CO3) and heat treatments (40 or 70 °C) on the functional properties of MBPI at high protein levels, for potential application as a plant‐based emulsion. The combined treatments reduced the zeta potential of protein suspensions from −9 to −19 mV and altered the protein conformation to form smaller particles (from 426 to 166 μm) with increased β‐sheet content. These treatments improved dispersibility of 8% MBPI suspension (58 to 86%), emulsifying activity index (6.34–10.89 m2 g−1), and stability coefficient (43 to 96%). Notably, MBPI samples treated with 0.3% Na2CO3 at 40 and 70 °C exhibited excellent emulsifying properties, forming stable monolayers at the oil–water interface, likely due to the increased surface activity of MBPI. Increasing protein concentration to 11% facilitated heat‐set gel formation; however, addition of 3.5%‐Na2CO3 induced premature gelation, limiting its application in emulsions. At 0.3%‐Na2CO3, increasing the protein content from 8% to 11% and the oil content from 10% to 30% further reduced emulsion droplet size, especially for MBPI treated with 0.3% Na2CO3 at 70 °C (MB‐0.3%‐70 °C) from 5.10 to 2.61 μm, likely due to decreased coalescence. This treatment yielded superior MBPI‐stabilised emulsion gels with enhanced penetration, fluid retention, and stability by possibly reducing protein aggregation. These findings demonstrate the potential of MBPI modified by combined addition of 0.3% Na2CO3 and heat treatment, particularly MB‐0.3%‐70 °C, as a promising ingredient for producing plant‐based emulsions.

Binding mechanism and structural characteristics of alloyed protein complex for enhanced solubility of hemp seed protein isolate

Despite the numerous health benefits and high digestibility of hemp seed protein isolate (HPI), its low solubility at neutral pH limits its utilization in the food industry. Therefore, we subjected insoluble HPI and soluble mung bean protein isolate (MBPI) to pH co-shifting under extremely alkaline conditions to form an alloyed protein complex (A-HM). At a mass ratio of HPI:MBPI of 50:50, A-HM exhibited the highest solubility (95.30 ± 0.99 %), and also had high resistance to heat treatment. Native PAGE demonstrated the formation of alloyed protein complexes, and particle size analysis revealed that A-HM exhibited small particle sizes and dispersion in water without aggregation of HPI. Owing to their small size, numerous hydrophobic residues and aromatic ring of HPI were exposed on the surface. Hydrophobic interactions predominantly governed the binding force involved in the formation of A-HM. Our findings may enhance HPI applications in the food industry, particularly in plant-based beverages.

Low-moisture extruded mung bean protein isolate and wheat gluten: Structure, techno-functional characteristics and establishment of rehydration kinetics of the products

Low-moisture extruded products provide excellent shelf-life and stability, making the exploration of new formulations with various proteins highly valuable. This study prepared and compared products with different ratios of mung bean protein isolate (MPI) to wheat gluten (WG) (10:0, 9:1, 8:2, 7:3, 6:4, and 5:5). Results showed significant improvements (P < 0.05) in L∗-value and product quality with increasing WG ratios, peaking at an MPI/WG ratio of 7:3. Increased WG also enhanced protein cross-linking aggregation, as evidenced by changes in particle size, secondary structure, and fluorescence spectra. However, excessive WG (MPI/WG = 6:4) adversely affected product structure and techno-functional characteristics. Rehydration kinetics were best described by the Peleg model, with rehydrated products showing decreased hardness (291.25 N) and chewiness (227.45 N), but increased tensile resistance (P < 0.05). Eleven quadratic polynomial equations were developed to predict color and techno-functional characteristics based on WG percentage (0–50%). The findings provide a theoretical basis for expanding the application of MPI in new low-moisture extruded products.

Comparing gluten‐free eggless muffins' viscoelastic, rheological, and textural properties after combining seven plant‐based protein isolates with wheat, corn, and rice starches

SummaryThis study aimed to substitute egg albumin with eight plant‐based protein isolates and xanthan gum for the development of gluten‐free, eggless muffins. The presence of protein isolates led to reduced pasting viscosities, suggesting limited swelling capacity of the starch granules. Incorporating different protein isolates enhanced the batter's viscoelastic properties, marked by an increase in storage and loss modulus and a decrease in tan δ, indicating enhanced gel properties compared to starch‐only batters, which showed more liquid‐like characteristics. Consequently, the muffins exhibited greater specific volume, springiness, and cohesiveness. The consistency of the muffins varied depending on the protein isolates used. The inclusion of protein isolates also altered the crust's hue, shifting it towards a reddish‐brown shade, while the crumb colour varied with protein incorporated. Sensory evaluation demonstrated that overall acceptability of the muffins improved with the protein isolates, particularly for those incorporating mung bean protein isolate. Principal Component Analysis further highlighted the strong associations between specific quality attributes, underscoring the significant impact of protein isolates on the quality characteristics of gluten‐free muffins.

Techno-functional properties and allergenicity of mung bean (Vigna radiata) protein isolates from Imara and KPS2 varieties

Mung bean is an increasingly cultivated legume. This study compared mung bean varieties ‘KPS2’ from Thailand (Th) and ‘Imara’ from Tanzania (T) with a focus on protein composition, allergenicity, and techno-functional properties. Two rounds alkaline-acid extraction were performed to produce mung bean protein isolate (MBPI - Th1/T1 and Th2/T2), supernatant (S) and protein-poor residue (PPR). Mass spectrometric analysis revealed high abundance of 8 s-vicilin and 11 s-legumin in MBPI and S. Extraction removed considerable amounts of the seed albumin allergen but increased the relative abundance of cupins in MBPI. Higher vicilin levels were found in Th1 samples, contributed to increased protein solubility above pH 6.5. Th formed stronger gels which were more stable at higher frequencies. In contrast, T proteins were structurally more flexible, leading to its improved foaming ability. This study provides the knowledge and methods for appropriate selection of mung bean varieties for various food applications.

Effect of transglutaminase on gelation and functional proteins of mung bean protein isolate

This study aimed to improve mung bean protein’s gelation qualities via microbial transglutaminase (mTGase) cross-linking. The mTGase treatment significantly improved gel hardness and storage modulus (G′) at higher enzyme levels (2 IU/g), peaking hardness at 3 h. The scanning electron microscopy imaging demonstrated more cross-linked structures at 2 IU/g, evolving into a dense network by 3 h. The water-holding capacity for mTGase-treated samples (2 IU/g, 3 h, 55 °C) tripled to 3.77 ± 0.06 g/g versus control (1.24 ± 0.02 g/g), alongside a 15 % decrease in zeta potential (−30.84 ± 0.901 mV versus control’s −26.63 ± 0.497 mV) and an increase in emulsifying activity index to 4.519 ± 0.004 m2/g from 3.79 ± 0.01 m2/g (control). The confocal images showed a more uniform lipid droplet distribution in mTGase-treated samples, suggesting enhanced emulsifying activity. Thus, mTGase treatment significantly improved gel strength and emulsifying properties, making it ideal for plant-based seafood products.

Improvement of processable properties of plant-based high internal phase emulsions by mung bean protein isolate based on pH shift treatment.

High internal phase emulsions (HIPEs) are unique emulsion systems that transform liquid oil into solid-like fats, thus avoiding the use of saturated fat and leading to a healthier and more sustainable food system for consumers. HIPEs with oil volume fraction (ϕ) of 75-85% were fabricated with mung bean protein isolate (MPI) under different pH shift treatments at 1.0% concentration through the one-step method. In the present study, we investigated the physical properties, microstructures, processing properties, storage stability and rheological properties of HIPEs. The results suggested that the properties of MPI under different pH shift treatments were improved to different degrees, stabilizing HIPEs (ϕ = 75-85%) with various processability to meet food processing needs. Under alkali shift treatment conditions, the particle size of MPI was significantly reduced with better solubility. Moreover, the exposure of hydrophobic groups increased the surface hydrophobicity of MPI, awarding MPI better emulsifying properties, which could stabilize the HIPEs with higher oil phase fraction. In addition, the MPI under pH 12 shift treatment (MPI-12) had the best oil-carrying ability to form the stable HIPEs with oil volume fraction (ϕ) up to 85%, which was the highest oil phase in preparing the HIPEs using plant protein solely at a low concentration under neutral conditions. A series of stable HIPEs with different processing properties was simply and feasibly fabricated and these are of great potential in applying edible HIPEs. © 2024 Society of Chemical Industry.

Characteristics of Pickering emulsions stabilized by microgel particles of five different plant proteins and their application

Pickering emulsions stabilized by protein particles are of great interest for use in real food systems. This study was to investigate the properties of microgel particles prepared from different plant proteins, i.e., soybean protein isolate (SPI), pea protein isolate (PPI), mung bean protein isolate (MPI), chia seed protein isolate (CSPI), and chickpea protein isolate (CPI). MPI protein particles had most desirable Pickering emulsion forming ability. The particles of SPI and PPI had similar particle size (316.23 nm and 294.80 nm) and surface hydrophobicity (2238.40 and 2001.13) and emulsion forming ability, while the CSPI and CPI particle stabilized emulsions had the least desirable properties. The MPI and PPI particle stabilized Pickering emulsions produced better quality ice cream than the one produced by SPI particle-stabilized emulsions. These findings provide insight into the properties of Pickering emulsions stabilized by different plant protein particles and help expand their application in emulsions and ice cream.

Dry fractionation of Australian mungbean for sustainable production of value‐added protein concentrate ingredients

AbstractBackground and ObjectivesDry fractionation, combining milling and air classification technology, offers an economical and sustainable pathway for the processing of value‐added protein ingredients from Australia's major pulse crops. Leveraging a wider range of pulses will help meet the growing demand for plant‐based protein ingredients. This study demonstrates the efficient processing of protein concentrates from Australian mungbean, which were characterized for key nutritional properties, phytochemical constituents, protein quality, and protein secondary structure.FindingsMilling and air classification of mungbean flour resulted in protein concentrates (fine fraction) with a protein content of 62.2 g/100 g (db), reflecting a two‐fold increase in protein content compared to the original flour (p &lt; .05). Ash, fat, dietary fiber, and free phenolic and antioxidant compounds, also co‐concentrated with protein in the fine fraction (p &lt; .05), imparting enhanced nutritional properties with the potential to deliver health benefits. The protein quality of dry fractionated mungbean protein concentrate was compared to a commercial source of mungbean protein isolate (88 g/100 g, [db]). Amino acid scores highlighted deficiencies in sulfur‐containing amino acids, methionine, and cysteine, as well as tryptophan and threonine. In vitro protein digestibility‐corrected amino acid scores for the mungbean protein concentrate and protein isolate were 63.7% and 59.5%, respectively. SDS‐PAGE protein profiles showed no major differences in protein composition, indicating that no specific types of proteins are lost during the dry fractionation process. Fourier transform infrared analysis of protein secondary structure showed that β‐sheets were the dominant structural component, with relative percentages of 36% and 49%, for the mungbean protein concentrate and isolate, respectively.ConclusionsThere is significant potential for dry fractionation to deliver value‐added opportunities for Australian mungbean, through the production of protein concentrate ingredients with enhanced nutritional properties for use in new and existing foods.Significance and NoveltyNutritional properties, protein quality, and protein secondary structure were compared for protein concentrates and protein isolates processed from Australian‐grown mungbean. Key findings from this study will inform pulse protein processors and pulse‐based food manufacturers.

Determination of Thermal Conductivity Constant for Spray-Dried Mung Bean Protein Isolate using Series-Parallel “Block” Method and Central Composite Design

The efficient production of mung bean protein isolate (MBPI) is essential for sustainable food processing, yet it is energy-intensive due to drying phase required to convert raw mung beans into a fine powder. This work was carried out to calculate the thermal conductivity constant (k) of protein (A), moisture (B) and residual carbohydrate (C) of spray-dried MBPI. The protein slurry was prepared by dissolving MBPI in water at the ratio of 1:3, 1:4, and 1:5 prior to spray drying. The protein slurry was then spray dried at three different inflow temperatures of 140, 160, and 180 °C. A Series and Parallel Combination "Block" Model in tandem with a Central Composite Design (CCD) were selected to calculate the thermal conductivity constant of A, B and C. Eight arrangement components on A, B, and C component, measurements were derived from the initial three data points by utilizing the CCD method, in the preliminary study. By utilizing the series-parallel approach and statistical combination, there are a total of forty study arrangements. The thermal conductivity of MBPI with arrangements of A, B, and C (pABC); and a series of combinations of A and C in parallel to B (sAC pB) ranged from 0.1964-0.224 Wm-1 ℃ -1, with R2 = 98.73%-99.42%. Therefore, the energy requirement of spray drying process for MBPI could be predicted by the thermal properties of each component selected in the protein isolate.

Structural and functional characterization of mung bean protein-peach gum conjugate through the Maillard reaction as a novel encapsulation agent

This study used peach gum (PG) and mung bean protein isolate (MBPI) as an encapsulation agent. This study used peach gum (PG) and mung bean protein isolate (MBPI) as an encapsulation agent. The present investigation was undertaken to examine and refine the conjugation process of MBPI-PG, while concurrently evaluating the impact of Maillard modification on functional properties through the wet heat method. Through the analyses of SDS-PAGE, glycation degree, SEM micrographs, and FT-IR spectroscopy, it was ascertained that optimal glycosylation conditions were achieved at a pH of 8.5 and a temperature of 90 °C for a duration of 1 h. Conjugation resulted in the enhanced of solubility, emulsifying properties, and DPPH radical scavenging activity of MBPI. In comparison to their un-conjugated one, the observed improvements in thermal stability and solubility of proteins were attributed to the process of glycation. Collectively, the findings imply that the conjugation with PG imparts additional functional attributes to MBPI, thereby potentially enhancing its applicability in the food industries as a novel encapsulation agent.

Effect of pH-shifting on the water holding capacity and gelation properties of mung bean protein isolate

In this study, alkaline pH-shifting modified the globular structure of mung bean protein isolate (MBPI) to form flexible and stretched structures. In contrast, acidic pH-shifting increased the rigidity of MBPI. The increased flexibility (at the level of the secondary structure) and newly exposed intermolecular amino acid groups induced by alkaline pH-shifting improved the water holding capacity and gelation properties of proteins. Specifically, MBPI treated at pH 12 (MP12) showed the most flexible structure and highest water holding capacity and gel formation properties (least gelation concentration). The water-holding capacity of native MBPI increased from 1.56 g/g to 4.81 g/g, and its least gelation concentration decreased from 22 % to 15 % by pH-shifting at pH 12. Furthermore, MP12 formed stronger and more elastic heat-induced gels than native MBPI. We identified significant differences in the structural properties and water holding capacity, and gelation properties of acidic and alkaline pH-shifted MBPI and investigated the gelation properties of MP12 including rheological and morphological analyses. Our findings can facilitate the use of mung beans as a protein source in a wide range of food applications, including plant-based and processed meats.

Effect of l-cysteine on functional properties and fibrous structure formation of 3D-printed meat analogs from plant-based proteins

The development of three-dimensional (3D) printed meat analogs with fiber, texture, and sensory resembling meat remains challenging. This study investigated the effect of l-cysteine on functionality enhancement and fibrous structure formation in mixtures of mung bean protein isolate (MBPI) and wheat gluten (WG) for meat analog production. 3D printing was used to construct fibrous filaments. Raw MBPI-WG mixtures decreased rheological properties when increasing l-cysteine contents (0.0%–0.6%), promoting ink extrudability. The cys-0.4% ink exhibited the highest printing resolution and structural stability, correlated with its higher mechanical strength and increased disulfide cross-links. After cooking, the cys-0.4% sample showed a pronounced fibrousness in agreement with its microstructure image. This meat analog displayed a muscle-meat-like structure, improved texture, and reduced beany odor and bitter taste. Excessive cysteine contents (0.5%–0.6%) negatively affected the functionality of meat analogs. This study provides guidance for optimizing the amount of l-cysteine in meat analogs to improve product quality.

Molecular characterization and allergenicity assessment of different samples of Mung Bean

Legumes represent a promising nutritional alternative source of proteins to meat and dairy products. Additionally, Novel Foods (Regulation EU 2015/2283) can help meet the rising protein demand. However, despite their benefits, emerging allergenicity risks must be considered. The aim of this work is the molecular characterization of the Novel Food Mung bean protein isolate for allergenicity prediction with High Resolution Mass Spectrometry analysis. The assessment of the allergenicity was evaluated in silico by comparing protein sequences of the Novel Food with other known legume allergens, using bioinformatic databases. The results highlighted similarity higher than 60 % of the protein structure of Mung bean with two known allergens of soybean and pea. Furthermore, enzymatic hydrolysis effects on allergenic potential was evaluated by immunoblotting analysis using sera of patients allergic to legumes. The protein hydrolysates obtained showed a high nutritional quality and a reduced allergenic potential, making them suitable for hypoallergenic food formulations.

Effect of ultrasonic assisted grafting on the structural and functional properties of mung bean protein isolate conjugated with maltodextrin through maillard reaction

Four different methods of maillard reaction including ultrasound (150 W, 10 min) assisted, classical wet heating (80 °C, 60min), moderate water bath heating (60°C, 12 to 30 h) and dry state method (60 °C, 79 % relative humidity and 48 h) were used to Mung bean protein isolate – Maltodexrtin conjugates (MPI-MD) preparation. The samples prepared under ultrasound and wet heating were chosen for further analysis according to degree of graft and UV-absorbance at 420 nm. Higher glycosylation at short time and lower browning were obtained under ultrasound treatment. Covalent attachment in conjugates confirmed by SDS-polyacrylamide gel electrophoresis. The structural analysis revealed prominent unfolding effect of ultrasound waves on the protein's molecules. The decrease of α-helix content was related to the exposure of buried amino group residues during reaction. Glycation of MPI under ultrasound caused changes in tertiary structure of protein and leads to decrease in the fluorescence intensity compared with native and wet heating treatments. FTIR spectra confirmed the conjugation of the MPI and MD and suggested that protein structure was changed and ultrasound promoted the graft reaction more than wet heating treatment. Conjugated MPI showed higher emulsification and solubility index than MPI, moreover the effect of ultrasonic waves on ameliorated functional properties was impressive than those for wet heating treatment. Overall, this study showed use of ultrasonication in maillard reaction was a suitable method for producing MPI- MD conjugates and improved the efficiency of graft reaction and functional properties of grafts.

Mungbean and pumpkin protein isolates as novel ingredients for the development of meat analogs using heat-induced gelation technique

Mungbean and pumpkin are rich source of proteins and nutrients which could be utilized in novel food formulations. This study involves formulation of meat analog using mungbean protein isolate (MBPI) and pumpkin protein isolates (PPI) through optimization process using Box–Behnken Design (BBD) of response surface methodology (RSM). MBPI and PPI were used as base ingredients for the development of meat alternatives using an innovative heat-induced gelation process. Methylcellulose (MC) and gum Arabic were used as supporting matrices for obtaining desired texture of the meat analog. The emulsifying activity, water-holding capacity, and oil-holding capacity of MBPI and PPI were analyzed. The set of physicochemical response factors used in RSM was moisture content, protein content, color, and textural properties of the formulated meat analogs. The selected independent variables were set at three levels (−1, 0, 1) with protein ratio (20:10, 15:15, and 10:20 of MBPI-PPI), Water (32, 37, and 42%), and MC (5, 6, and 7%). RSM results showed that the model effectively described the correlation between the independent variables (protein ratio, water percentage, and MC percentage) and the response factors. The microstructure of the analog showed porous and fibrous structures. It was observed that the degree of cross-linking between protein molecules could have impacted the textural properties that were associated with viscoelastic characteristics as reflected in the rheological analysis. Overall, the study shows that the mungbean and pumpkin seed proteins could be utilized as a potential ingredient to improve the textural properties of the meat analog, while it is also recommended to explore such proteins with other mechanical processing techniques like extrusion.

Hybrid Paneer: Influence of mung bean protein isolate (Vigna radiata L.) on the texture, microstructure, and in vitro gastro-small intestinal digestion

Replacing dairy proteins with legume proteins such as mung bean protein can create hybrid cheese alternatives with superior nutritional and functional properties. The effects of partially replacing (30%) cow milk with mung bean protein isolate (MBPI) on the rheology, texture, microstructure, and digestibility of paneer (acid-heat coagulated cheese) were studied. The developed hybrid cow milk-mung bean paneer (CMMBP) had higher protein and moisture contents, lower fat content, and a darker colour than cow milk paneer (CMP). CMMBP showed a significant reduction in hardness, cohesiveness, chewiness, and springiness compared to the cow milk-based control. Frequency sweeps performed using a dynamic rheometer showed higher storage modulus (G′) for CMMBP compared to CMP, indicating greater elastic properties of the hybrid paneer. In vitro digestibility of CMMBP was significantly lower than CMP, as shown by the lower overall ninhydrin-reactive free amino N release and the presence of resistant peptides at the end of digestion.

Effect of Microbial Transglutaminase Treatment on the Techno-Functional Properties of Mung Bean Protein Isolate.

The purpose of this study was to investigate the improvement in techno-functional properties of mung bean protein isolate (MBPI) treated with microbial transglutaminase (MTG), including water- and oil-holding capacity, gelling properties, and emulsifying capacity. MBPI dispersions were incubated with MTG (5 U/g of protein substrate) at 45 °C with constant stirring for 4 h (MTM4) or 8 h (MTM8). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that MTG treatment for different durations increased the amount of high-molecular-weight proteins in MBPI, and most of the cross-linking by MTG was terminated at 8 h. Improved water-holding capacity, gelling properties, emulsifying capacity, and stability were observed after MTG treatment, and decreased protein solubility and surface hydrophobicity were observed. Furthermore, the texture of the heat-induced gels made from MTG-treated MBPI was evaluated using a texture analyzer. MTG treatment increased the hardness, gumminess, chewiness, and adhesiveness of the heat-induced gels. Field-emission scanning electron microscopy demonstrated the enhanced hardness of the gels. This research reveals that MTG-catalyzed cross-linking may adjust the techno-functional properties of MBPI, allowing it to be used as a soy protein alternative in food products, such as plant-based and processed meats.

Mung bean protein isolate treated with high-intensity pulsed electric field: characteristics and its use for encapsulation of Asian seabass oil

Aim To modify the techno-functional properties of mung bean protein isolate (MBPI) by high-intensity pulsed electric field (HIPEF) treatment and to apply the treated MBPI for encapsulation of Asian seabass oil (ASO). Methods MBPI was prepared using isoelectric precipitation. HIPEF was applied to MBPI solutions at 25 kV/cm with varying pulse numbers (0–400). Physicochemical properties and structure of MBPI were assessed. ASO microcapsules prepared using HIPEF-treated protein as wall material was characterised and tested for storage stability. Results Solubility, surface hydrophobicity, total sulfhydryl content, and emulsifying property of MBPI increased and β-sheets and α-helix were altered after HIPEF treatment at pulse number of 300. ASO microcapsules possessing spherical shape with surface indentations had EE of 72.07 ± 5.08%. ASO capsules had lower lipid oxidation than the control during storage. Conclusion HIPEF improved techno-functional properties of treated MBPI. Treated MBPI could be used as wall material for encapsulation of fish oils.