Commercial Soy Protein Isolate Research Articles

Physicochemical Properties, Functionalities, and Antioxidant Activity of Protein Extracts from New Zealand Wild Sea Cucumbers (Australostichopus mollis).

This study investigated the physicochemical properties, functionalities, and antioxidant capacities of protein extracts from wild sea cucumber Australostichopus mollis collected from four distinct locations in New Zealand. Protein was extracted from sea cucumber body walls using trypsin enzymatic extraction, followed by cold acetone precipitation. The amino acid analysis revealed high glycine (189.08 mg/g), glutamic acid (119.45 mg/g), and aspartic acid (91.91 mg/g) concentrations in all samples. The essential amino acid indexes of the protein extracts (62.96, average) were higher than the WHO/FAO standard references, indicating the excellent protein quality of A. mollis. Furthermore, protein extracts from A. mollis demonstrated superior emulsifying activity (202.3-349.5 m2/g average) compared to commercial soy and whey protein isolates under all tested pH conditions, and enhanced foaming capacity (109.9-126.4%) and stability (52.7-72%) in neutral and acidic conditions. The extracts also exhibited good solubility, exceeding 70% across pH 3-11. Antioxidant capacities (ABTS and DPPH free radical scavenging activity and ferric reducing antioxidant power) were identified in A. mollis protein extracts for the first time, with clear variations observed among different locations. These findings elucidate the advantageous functional properties of protein extracts from wild New Zealand A. mollis and highlight their potential application as high-quality antioxidant food ingredients.

Effects of pH and temperature on the properties of acid-induced commercial soy protein isolate gel

The goals of this study were to investigate the effect of preheating conditions on the formation of thermal aggregates of commercial soy isolate protein (SPI) and to characterize the textural properties and microstructure of acid-induced SPI gels. SPI was subjected to preheating treatments at different temperatures (85 °C, 95 °C) and pH values (7.0, 7.5, 8.5, 9.5), and the treated SPI was then used to form acid-induced gels. Characterization of the different gels showed that lower temperatures and pH values favored protein aggregation and the formation of larger aggregates, while higher temperatures and pH values led to a lower degree of aggregation and the formation of smaller aggregates. The lowest average particle size (340.77 nm) and turbidity (0.063), and the highest solubility (81.79 %) were obtained when the preheating temperature of the thermal aggregates was 95 °C and the pH was 9.5. Higher preheating temperature and pH values caused the unfolding of SPI’s tertiary structure, decreased the content of β-sheet structure, and increased the exposure of hydrophobic groups and free sulfhydryl groups. These exposed groups facilitated protein–protein interactions during network assembly, resulting in denser and stronger gel networks. Notably, SPI subjected to higher temperatures and pH values exhibited greater binding capacity for water molecules, higher water holding capacity, and gel strength. Overall, the results showed that modification of preheating temperature and pH can control the formation state of SPI thermal aggregates, ultimately impacting the properties of SPI acid-induced gels.

Relating the protein denaturation degree and solubility of soy protein isolates to the structure of high moisture extrudates

Commercial soy protein isolates (SPI) with high protein denaturation degrees and low solubilities are often used raw materials for the production of meat analogues with high moisture extrusion (HME). The impact of such SPI properties on structure formation and protein-protein interactions/reactions that occur during HME processing is not well-understood. Therefore, SPI with (i) native and soluble proteins, (ii) denatured and aggregated proteins or (iii) blends thereof were subjected to lab-scale HME processing. Most native and soluble SPI proteins took part in the formation of new non-covalent interactions and disulfide bonds during HME processing, which resulted in a layered extrudate microstructure. In addition, even after disruption of non-covalent and covalent bonds, high MW aggregates (>100 kDa) were present in the extrudate. SPI with highly aggregated protein had low protein extractability and HME did not cause a pronounced further reduction in this regard. HME did, however, result in the formation of a fibrous extrudate structure. Extrusion of blends with intermediate content of both SPIs resulted in the highest extrudate hardness and cutting strength. These findings demonstrate a significant impact of SPI protein denaturation degree and solubility on high moisture extrudate structure and texture. Hence, in-depth evaluation of the protein physical properties of raw materials used for HME processing will aid in controlling product properties.

Alkaline solubilization of microalgal protein and its impact on the functional properties of protein extract

Microalgal alternative proteins are increasingly recognized as a sustainable and promising source for future food production. Despite the widespread use of alkaline solubilization in protein extraction, its influence on the functional properties of microalgal protein extracts has received limited attention. This study marks the pioneering effort to assess the impact of alkaline (NaOH) solubilization on both the extraction process and the functional properties of Chlorella vulgaris protein extract (CVPE) obtained through isoelectric precipitation. With the gradual escalation of alkaline concentration from 0 to 0.7 M, there was a notable improvement in protein extraction efficiency, increasing significantly from 6.22 % to 56.23 %. However, elevated NaOH concentrations resulted in protein degradation, as evidenced in SDS-PAGE studies. Alkaline solubilization exhibited a positive impact on various functional properties of CVPE. It enhanced solubility, water absorption capacity, foaming capacity and stability, as well as emulsifying activity and stability. However, there was a slight decrease in oil absorption capacity with increasing NaOH concentration. Notably, the maximum solubility, oil adsorption capacity, foaming capacity, and emulsion activity of CVPE were 2.3-, 1.8-, 2-, and 1.3-fold higher, respectively, than those of commercial soy protein isolate (SPI). This highlights the effectiveness of alkaline solubilization in modifying C. vulgaris protein and emphasizes the high potential of CVPE as a functional food ingredient.

Effect of Nonprotein Components for Lipid Oxidation in Emulsions Stabilized by Plant Protein Extracts.

Plant protein ingredients are rich in non-protein components of which the antioxidant and pro-oxidant effects are expected to be considerable. In this paper, commercial soy and pea protein isolates and concentrates were selected by using their soluble fractions to prepare oil-in-water (O/W) emulsions. Emulsions stabilized with soy protein isolates were more prone to lipid oxidation than those with soy protein concentrate or pea protein isolate. Compositional analysis revealed that the soluble fraction of soy protein isolates contained higher concentrations of phenolic compounds and metals (iron and copper) but lower mineral and ash contents than those of soy protein concentrate and pea protein isolate. Correlating the composition to oxidation in emulsions highlighted the significant role of non-protein components, alongside the protein's oxidative state. These findings are relevant for the use of alternative proteins in food formulation, a practice often promoted as sustainable yet that may come with repercussions for oxidative stability.

Effects of alkaline and ultrasonication on duckweed (Wolffia arrhiza) protein extracts’ physicochemical and techno-functional properties

Wolffia is a protein-rich aquatic plant with the potential to help address food sustainability issues; however, a more efficient extraction process must be sought due to limited yield with conventional methods. This study aimed to investigate the effects of duckweed forms (fresh and dried), duckweed-to-aqueous solution ratio (DSR), as well as alkaline and ultrasonication extractions on yields, physicochemical and techno-functional properties of duckweed protein extracts (DPE). Three extraction methods were used: alkaline extraction (AE), ultrasound-assisted alkaline extraction (UAAE), and ultrasound-assisted water extraction (UAWE). The study showed fresh duckweed resulted in a 2.5-fold higher yield and protein recovery than oven-dried duckweed. UAE significantly enhanced extraction yield and protein recovery. The optimal extraction process was a DSR of 1:6 using UAAE at pH 8.5, resulting in a 16% yield and 34% protein recovery. Furthermore, the study found that UAE facilitated the extraction of non-polar/hydrophobic amino acids while AE proved to be efficient in extracting sulfur-containing amino acids. This study, for the first time, revealed the role of UAE and AE in promoting the extraction of different profiles of amino acids. The DPE produced using UAAE contained 65% protein, meeting the WHO/FAO/UNU recommended protein intake for preschool-aged children. Furthermore, the DPE exhibited excellent emulsifying properties and oil-holding capacity comparable to commercial soy protein isolates. Overall, UAAE was identified as a promising approach for producing techno-functional and nutritious protein ingredients from Wolffia. The resulting DPE proved to show great potential for functional plant-based food and feed applications.

Hemp (Cannabis sativa L.) protein: Impact of extraction method and cultivar on structure, function, and nutritional quality

Hemp (Cannabis sativa L.) is increasingly gaining traction as a novel and sustainable source of plant protein. Accordingly, the aim of this study was to investigate the effectiveness of two protein extraction methods, alkaline extraction coupled with isoelectric precipitation (AE-IEP) and salt extraction coupled with ultrafiltration (SE-UF) in producing hemp protein isolates (pH-HPI and salt-HPI) with high purity and yield. Structural characterization as impacted by extraction method and cultivar was performed and related to functional performance and nutritional quality. Both extraction methods, with carefully selected parameters, resulted in HPI with high purity (86.6–88.1% protein) and protein extraction yields (81.6–87.3%). All HPI samples had poor solubility (∼9–20%) at neutral pH compared to commercial soy protein and pea protein isolates (cSPI, cPPI). A relatively high surface hydrophobicity and low surface charge contributed to such poor solubility of HPI. However, HPI demonstrated similar solubility at acidic pH (50–67%) and comparable gel strength (up to 24 N) to cSPI. Comparing experimental amino acid composition to the theoretical amino acid distribution in hemp protein provided insights to the functional performance of the protein isolates. While pH-HPI demonstrated better functionality than salt-HPI, minimal structural, functional, and nutritional differences were noted among the pH-HPI samples extracted from four different cultivars. Overall, results from this work could be used to guide future attempts to further develop successful protein extraction processes, and to provide valuable insights to propel breeding efforts that target enhanced hemp protein characteristics for food applications.

Different source of commercial soy protein isolates: Structural, compositional, and physicochemical characteristics in relation to protein functionalities

This study aimed to illustrate the relationship among physicochemical properties, subunit composition and protein functionalities in a broad collection of commercial soy protein isolates (SPIs) from China and the EU. The results indicated that SPIs had large variations in glycinin/β-conglycinin composition, protein denaturation, and water- and oil-binding capacity (WBC and OBC) and solubility. These SPIs could be roughly divided into pre-denatured SPI, partially hydrolyzed SPI, and less modified SPI. The pre-denatured SPI with high surface hydrophobicity and large particle sizes showed reduced WBC and OBC due to increased protein aggregation, and partially hydrolyzed SPI showed high protein solubility owing to the exposure of hydrophilic regions and reduction in molecular size. The processing-induced physicochemical changes played a pivotal role in determining protein functionalities, whereas subunit composition affected protein functionality less. Overall, this study highlighted the obvious difference in raw material quality of commercial SPI, and provided promising methods for SPI categorization.

Impact of extraction conditions and seed variety on the characteristics of pennycress (Thlaspi arvense) protein: a structure and function approach

AbstractAs the consumer demand for plant proteins continues to grow, the food industry is seeking novel and sustainable protein sources to incorporate in various food products. Pennycress (Thlaspi arvense), a sustainable cover crop, produces oilseeds high in protein, warranting investigation. Accordingly, protein extraction from pennycress was evaluated under various extraction conditions, using alkaline extraction and salt solubilization coupled with ultrafiltration. Given the superior color and functionality of the salt extracted pennycress protein isolate (PcPI), its production was scaled‐up about two hundred folds in a pilot plant. Furthermore, a new pennycress accession bred to have zero erucic acid (0EA) was evaluated to determine the impact of seed variety on protein characteristics. Structural and functional characterization was performed on PcPI and compared to native (nSPI) and commercial (cSPI) soy protein isolates. Salt extracted PcPI had comparable gel strength to cSPI, three times higher solubility under acidic conditions, and ~1.5 times better emulsification capacity. PcPI extracted from 0EA was mildly different in structure and functionality from that extracted from wildtype pennycress, with the slight variation attributed to genetic variance. Finally, the protein digestibility‐corrected amino acid score (PDCAAS) of the salt extracted PcPI, calculated in vivo (0.72) and in vitro (0.87), was superior or comparable to other plant protein sources. This research provided, for the first time, a comprehensive evaluation of different protein extraction protocols to produce a functional PcPI that can compete with soy protein for various food applications, such as acidic beverages, meat and dairy products, and emulsified systems.

Rheological and textural properties of heat-induced gels from pulse protein isolates: Lentil, mungbean and yellow pea

The molecular structure and conformation of the plant-based proteins dominate their gelation behaviour. These aspects have been mostly overlooked for underutilised pulse proteins such as lentils and mungbean that differ structurally with soy and pea proteins. Rheological and textural properties of heat-induced gels of lentils (LPIs) (green, red and black lentils), mungbean (MBPI) and yellow pea (YPPI) were compared with commercial soy (CSPI) and pea (CPPI) protein isolates. On investigation of the dynamic rheological parameters, the critical protein concentration (CPC) of MBPI was the lowest (14% w/v) followed by LPIs (18% w/v) and YPPI (22% w/v). Also, vicilin-rich MBPI showed a lower gelation temperature (Tgel 77 °C) and developed stronger gels compared to LPIs and YPPI. On the other hand, commercial isolates with larger particle size, water holding capacity and denatured state showed lower CPC (CPPI, 14% w/v) than their folded and more soluble counterparts (YPPI 22% w/v). Hence, the study of thermo-rheological properties of pulse proteins with distinct molecular and conformation characteristics has yielded a structure-gelation paradigm. These findings support the development of plant protein-gelled products not limited to meat and dairy analogues.

The effects of tempe protein isolate from non-germinated and germinated soybean on oxidative stress in diabetic rats

Diabetes mellitus (DM) patients tend to be more susceptible to the COVID-19 virus. Evidence suggests that infection with the COVID-19 virus leads to increase reactive oxygen species (ROS) production. Moreover, hyperglycaemic conditions also produce excess ROS. Those can lead to oxidative stress in DM patients. This study aimed to prevent oxidative stress by using innovative functional food called tempe protein isolates, which were isolated from both non-germinated soybean (TPIN) and germinated soybeans (TPIG). TPIN, TPIG and commercial soy protein isolate (CSPI) were given 900 mg/kg BW to DM rats for 28 days. The DM rats were modelled by inducing an alloxan dose of 110 mg/kg BW intraperitoneally. Results showed there were no significant differences (p>0.05) in feed intake and blood profile. TPIN significantly prevented excessive weight loss and reduced blood glucose (p<0.05) better than TPIG and CSPI. TPIN and TPIG significantly (p<0.05) prevent the formation of MDA in the kidney, increase the activity of the SOD enzyme in both liver and kidney tissues and increase Cu,Zn-SOD antioxidant. This study concluded that the administration of TPIG and TPIN could prevent liver and kidney tissue damage by free radicals. Furthermore, TPIN has better potential than TPIG to prevent oxidative stress.

Salt Solubilization Coupled with Membrane Filtration-Impact on the Structure/Function of Chickpea Compared to Pea Protein.

The demand for pulse proteins as alternatives to soy protein has been steeply increasing over the past decade. However, the relatively inferior functionality compared to soy protein is hindering the expanded use of pulse proteins, namely pea and chickpea protein, in various applications. Harsh extraction and processing conditions adversely impact the functional performance of pea and chickpea protein. Therefore, a mild protein extraction method involving salt extraction coupled with ultrafiltration (SE-UF) was evaluated for the production of chickpea protein isolate (ChPI). The produced ChPI was compared to pea protein isolate (PPI) produced following the same extraction method in terms of functionality and feasibility of scaling. Scaled-up (SU) ChPI and PPI were produced under industrially relevant settings and evaluated in comparison to commercial pea, soy, and chickpea protein ingredients. Controlled scaled-up production of the isolates resulted in mild changes in protein structural characteristics and comparable or improved functional properties. Partial denaturation, modest polymerization, and increased surface hydrophobicity were observed in SU ChPI and PPI compared to the benchtop counterparts. The unique structural characteristics of SU ChPI, including its ratio of surface hydrophobicity and charge, contributed to superior solubility at both a neutral and acidic pH compared to both commercial soy protein and pea protein isolates (cSPI and cPPI) and significantly outperformed cPPI in terms of gel strength. These findings demonstrated both the promising scalability of SE-UF and the potential of ChPI as a functional plant protein ingredient.

Heat treatment in the presence of arginine increases the emulsifying properties of soy proteins

This study aimed to improve the emulsifying properties of commercial soy protein isolates (CSPIs). CSPIs were thermally denatured without additives (CSPI_H) and with arginine (CSPI_A), urea (CSPI_U), and guanidine hydrochloride (CSPI_G), which improve protein solubility to prevent aggregation. These additives were removed by dialysis, and the samples were lyophilized. CSPI_A resulted in high emulsifying properties. FT-IR analysis showed that the β-sheet content in CSPI_A was reduced compared to that of untreated CSPI (CSPI_F). Fluorescence analysis showed that the tryptophan-derived emission peak of CSPI_A shifted between CSPI_F and CSPI_H which was exposed to hydrophobic amino acid chains with aggregation. As a result, the structure of CSPI_A became moderately unfolded and exposed the hydrophobic amino acid chains without aggregation. The CSPI_A solution had a more reduced oil–water interface tension than other CSPIs. These results support that CSPI_A attaches efficiently to the oil–water interface and produces small, less flocculated emulsions.

Combination of pulsed electric field and pH shifting improves the solubility, emulsifying, foaming of commercial soy protein isolate

In this study, the effects of a new dual modification method, pulsed electric field (PEF) and pH shifting treatment, on the solubility, emulsifying and foaming properties of commercial soy protein isolate (SPI) were investigated. Results showed that the combination of PEF and pH shifting treatment, particularly at moderate PEF strength (10 kV/cm) and alkaline conditions (pH 11), facilitated protein structure unfolding and formation of smaller aggregates, substantially enhancing the solubility of SPI from 26.06% to 70.34%. Higher flexibility, surface hydrophobicity, and free sulfhydryl content were also found in the modified SPI, which boosted interfacial activity and significantly enhanced emulsifying and foaming properties. In alkaline environments, the enhanced functional properties of SPI at moderate PEF strength may be attributed to the appropriate oxidation of proteins by free radicals produced by electrochemical processes and the additional unfolding of protein conformations by polarization. The functional characteristics of SPI were decreased by an increase in PEF strength (20 kV/cm), which may be due to the tendency of the protein to aggregate and undergo excessive oxidation. This work may provide an effective methodological and theoretical basis for the modification of SPI by combining PEF and pH shifting treatment. • PEF combined with pH shifting treatment efficiently improved the solubility of SPI. • The treated SPI showed dramatic enhancement in emulsifying and foaming properties. • Enhanced unfolding in pH shifted SPI were observed after PEF introduction. • PEF-induced polarization and proper oxidation enhanced the functional property of SPI.

Effect of high-pressure jet processing on the structure and physicochemical properties of plant protein isolate aqueous dispersions

There is a strong interest in incorporating proteins from plant sources into protein-rich beverages. However, the use of protein isolates in food systems is restricted by their poor solubility and overall functionality. This research aimed to investigate the impact of high-pressure jet (HPJ) processing from 0 (control) to 500 MPa on the structural and physicochemical properties of three commercial soy protein isolates (SPIs) and pea protein isolates (PPIs) 5% w/v aqueous dispersions. Processing by HPJ at 100 MPa caused a strong dissociation of large protein bodies into smaller protein aggregates, following by a linear reduction in particle size when processing from 100 to 500 MPa. Native-PAGE of the supernatants showed that the molecular weight of the obtained soluble fractions was >250 kDa (no monomeric units), indicating the lack breakdown of protein covalent bonds. The reduction of the large protein bodies into small-size protein aggregates affected the overall functionality of the protein isolates. The solubility and the foaming capacity of plant proteins increased >15% as the aggregates dropped in size due to HPJ processing. The hydroxyl radical scavenging activity of PPIs increased >15% after pressurization, but HPJ did not influence the emulsion stability. The improvement in the physicochemical properties of plant-based proteins highlights the potential use of HPJ technology to create novel ingredients that feature clean label claims.

Structure – Function relationship of Australian Acacia seed protein concentrates: Amino acid composition, in vitro protein digestibility and molecular properties

The nutritional, functional, in vitro protein digestibility (PD), structural, and molecular properties of Acacia seed protein concentrates (ASPC) from three Acacia species (Acacia victoriae, A. coriacea and A. cowleana) were investigated and compared with a commercial soy protein isolate (SPI). The essential amino acid profile in ASPC, except for methionine, exceeded the minimum daily requirements for adults recommended by the FAO/WHO. The ASPC PD, particularly from A. victoriae and A. coriacea, was considerably high (64.2–79.3%), but lower than SPI (89.5%). ASPC proteins had higher molecular weights ranging from 50 to 65 kDa (associated with 7S vicilin subunit), better protein solubility and oil absorption capacity than SPI. Emulsifying properties were comparable between ASPC and SPI. Among the Acacia species, the proteins from A. victoriae and A. cowleana exhibited higher protein quality, foaming capacity and solubility compared to A. coriacea. Overall, ASPC from A. victoriae and A. cowleana showed potential as ingredients in food processing.

Jet cooking dramatically improves the wet strength of soy adhesives

AbstractThe impact of jet cooking on shear strength of soy‐and‐water adhesives was investigated to understand the higher shear strength of commercial soy protein isolates compared to soy flours. Soy flour‐based wood adhesives are appealing because of their bio‐based content, low formaldehyde emission, and low cost, but their commercial application is limited by low wet cohesive strength. Previous researchers proposed that the process of jet cooking (steam injection with high turbulence followed by rapid cooling) was responsible for the high (~3 MPa) wet shear strength of adhesives made with commercially produced soy protein isolate, using the ASTM D 7998 test. In this work, we show that jet cooking did dramatically increase the wet strength of laboratory‐produced, native‐state soy protein isolate from 0.6 to 3 MPa, a strength similar to many commercial isolates. Jet cooking was far less effective at developing wet strength of soy flours, but greatly increased the viscosity of virtually all our soy materials. We hypothesize that the benefits of jet cooking are primarily a result of nonequilibrium protein aggregation states because subsequent wet autoclaving of jet cooked soy proteins dramatically decreased wet strength. The dramatic differences in adhesive properties between commercial soy protein isolates and soy flours suggests that the common practice of using results obtained with commercial isolates to predict the performance of soy flour adhesives is inappropriate.

Effect of ultrasonic cavitation on the formation of soy protein isolate – rice starch complexes, and the characterization and prediction of interaction sites using molecular techniques

Protein-carbohydrate interactions occur naturally in glycoproteins which are highly stable in nature and are involved in various food complexes and can enhance the quality and functional properties of foods. In the current study, we characterized the protein-carbohydrate complex formed between commercial soy protein isolate and rice starch using different treatments namely heat treatment alone, ultrasound treatment alone, combination of ultrasound and heat treatment and mixing alone. The structural data obtained using circular dichroism indicated that during the complex formation, the α-helix values were reduced by a maximum of 67% compared to soy protein isolate alone. The crystalline nature of the complexes formed by ultrasound treatment preserved the techno-functional properties as compared to complexes formed by heat treatments. The FTIR analysis of the complexes formed indicated the formation of glycosidic bond. Molecular docking analysis revealed the interaction between the complexes occurred due to hydrogen bonds which make the proteins more stable in nature thus enhancing their denaturation temperature. Glutamine, Proline and Arginine present in the D subunit of 7S 3AUP interacts with the starch molecule. The obtained results suggest that sonication combined with heat treatment led to higher interaction between the soy proteins isolate and rice starch.

Optimization of Soybean Protein Extraction Using By-Products from NaCl Electrolysis as an Application of the Industrial Symbiosis Concept

Defatted soybean flour is generated during the oil extraction process of soybean, and it has a protein content of ~50%. On the other hand, an alkaline solution of NaOH is produced during the electrolysis process of NaCl in a novel method used to make a potent disinfectant/antiseptic (HOCl). In the present work, we suggest using these two products to produce soy protein isolate (SPI), aiming to create an industrial symbiosis. A Box–Behnken experimental design was executed, and a surface response analysis was performed to optimize temperature, alkaline solution, and time used for SPI extraction. The SPI produced at optimal conditions was then characterized. The experimental results fit well with a second-order polynomial equation that could predict 93.15% of the variability under a combination of 70 °C, alkaline solution 3 (pH 12.68), and 44.7 min of the process. The model predicts a 49.79% extraction yield, and when tested, we obtained 48.30% within the confidence interval (46.66–52.93%). The obtained SPI was comparable in content and structure with a commercial SPI by molecular weight and molecular spectroscopy characterization. Finally, the urease activity (UA) test was negative, indicating no activity for trypsin inhibitor. Based on the functional properties, the SPI is suitable for food applications.

Physicochemical and functional properties of pigeon pea (Cajanus cajan) protein and non-starch polysaccharides

Pigeon pea (Cajanus cajan L. Millsp) has been commonly consumed in human diet, and it is also a promising source of protein and dietary fibers. In this study, pigeon pea protein and non-starch polysaccharides (NSP) were sequentially extracted and fractionated. The amino acid profile of protein was characterized, and total sugars and uronic acid of non-starch polysaccharides were identified. Physicochemical properties of pigeon pea protein were compared with commercial soy protein isolates; meanwhile, pigeon pea NSP was compared with commercial citrus pectin. The results indicated that the viscosity of protein solution from pigeon pea is higher than that from soy protein isolates at all concentrations and exhibited shear-thinning behavior at shear rate range 0.1–500 s−1. The emulsions prepared from pigeon pea protein at the concentrations of 0.5% and 2% (w/w) displayed significant higher emulsifying stability (p < 0.05) than those of soy protein. Pigeon pea polysaccharide exhibited higher surface activity than citrus pectin, with the 0.5% pigeon pea polysaccharide solution comparable with 1.5% citrus pectin solution. The results of this study have implied great potentials of application of pigeon pea protein and non-starch polysaccharide as novel ingredients for food industries.