Protein Isolates from Bambara Groundnut (Voandzeia Subterranean L.): Chemical Characterization and Functional Properties

The physicochemical, functional, and thermal properties of protein isolates obtained from two varieties of Bambara groundnut were evaluated. Proteins were isolated using alkaline extraction (isoelectric precipitation [IEP]) and micellisation techniques. IEP recorded a higher protein yield (56.3–58.2 g/100 g) than the micellised protein (MP) (14.2 – 15.6 g/100 g). A similar trend was observed for the protein content of the isolates. The isolates contained a high level of lysine, arginine, and glutamic acid compared to soy protein. Minimum solubility of the flours of the two varieties occured at pH 5. MP isolates exhibited higher solubility than the corresponding isoelectric (IEP) isolates over all pH values. The micellised protein recorded superior functional characteristics than the isoelectric isolates. The micellised isolates also showed a significantly higher (P < 0.05) foam capacity and stability, oil and water absorption properties than the isoelectric isolate. The MP of both varieties also recorded significantly higher emulsifying properties-+ than their isoelectric protein isolates. The micellised protein also had better gelation properties than the isoelectric isolate. Micellised and isoelectric isolates did not reveal major differences in the electrophoretic patterns; both isolates had three major bands at 35.0, 43.0, and 112.0 kDa. The bands in the isoelectric protein isolate however, were well defined compared with the micellised isolate. All Bambara isolates were not dissociated by 1,4-Dithiothreitol (DTT) suggesting that they do not contain subunits linked by a disulphide bond. This suggests that 7S vicilin may be the major storage protein in Bambara groundnut isolates. Differential scanning calorimetry studies (DSC) of the two varieties of bambara groundnut proteins indicated that the thermograms of the micellised isolates have a higher denaturation temperature Td (97.9–108.4°C) than their corresponding isoelectric isolates (89.5–90.6°C).     

Improved extraction of disulphide‐rich bioactive proteins from soya hulls: characterisation of a novel aspartic proteinase

Soya hull, an underutilised coproduct of soya processing, was investigated as a source of disulphide‐rich bioactive proteins. A Viscozyme L‐assisted extraction method was developed to improve the yield of extracted proteins. The extracted proteins were identified by MALDI TOF–TOF MS, and the most abundant disulphide‐rich protein among identified proteins was purified and the enzymatic properties were evaluated. The results indicated that the Viscozyme L‐assisted extraction method extracted significantly (P < 0.05) more proteins (39.01%) than did the aqueous method (4.52%). The yield of the purified aspartic proteinase nepenthesin‐1‐like [Glycine max] (GmAPN1K) (the most abundant disulphide‐rich protein) is 570 mg Kg^?1. The specific activity of GmAPN1K was 62.1 U mg^?1 at pH 3.0 and 37 °C. The enzyme was optimally active at pH 3.0 and 55 °C. It was stable within pH range 3.0–10.0 and up to 55 °C, respectively, and was specifically inhibited by pepstatin A.     

Optimisation of bambara groundnut water extract and skim milk composition as cryoprotectant for increasing cell viability of Lactobacillus spp. using response surface methodology

Four legume water extracts, that is bambara groundnut, soya bean, red kidney bean and black bean as well as skim milk, were examined for their effectiveness in protecting Lactobacillus rhamnosus GG and Lactobacillus fermentum SK5 during the freeze‐drying and storage. Bambara groundnut water extract (BGWE) showed promising cryoprotective activity that was comparable to skim milk. BGWE and skim milk at 2–10% w/v and 5–20% w/v individually produced survival rates for both strains of 87–88%. To further optimise the synergistic cryoprotective medium, response surface methodology was employed. The optimal combination was 4.93% w/v BGWE and 11.68% w/v skim milk for L. rhamnosus GG and 5.17% w/v BGWE and 11.36% w/v skim milk for L. fermentum SK5 with survival rates of 95.17% and 94.36%, respectively. The storage life of freeze‐dried cells of both probiotics at 4 °C and 30 °C for 6 months was markedly improved when they were produced with these optimal combinations.     

Isoelectric protein precipitation from mild-acidic extracts of de-oiled sunflower (<Emphasis Type="Italic">Helianthus annuus</Emphasis> L.) press cake

Sunflower protein extraction using sodium chloride solutions allows high extraction yields at pH ~6 while preventing oxidation and covalent binding of phenolic compounds to the proteins, which usually occurs under alkaline conditions. Since protein solubility is enhanced at high NaCl concentrations, isoelectric precipitation had to be adapted in the present study besides developing subsequent desalting steps. Precipitation losses decreased from 62 to 31% with increasing NaCl (0.6–2.0 mol/L) and protein concentrations of the solution (6–14 mg/mL) and decreasing pH of precipitation (pH 4.5–3.0). Maximum yields were achieved at low temperature (8 °C) and upon instant acid addition. After adsorptive removal of co-extracted phenolics from the protein extracts, overall protein yields were considerably higher after precipitation at pH 3.5 compared with 4.5, but only slightly higher after washing of the precipitates. The physico-chemical properties of the protein isolates did not differ significantly except for the marked protein denaturation upon precipitation at pH 3.5. From the proposed process, light-coloured protein isolates of high purity (>98%) are obtained, which are suitable for food use.     

Identification by GeLC‐MS/MS of Trypsin Inhibitor in Sarcoplasmic Proteins of Three Tropical Fish and Characterization of Their Inhibitory Properties

Sarcoplasmic proteins from 3 fish species were fractionated by 50% to 70% ammonium sulfate precipitation. Lyophilized fractionated sarcoplasmic proteins of threadfin bream (TB‐SP), bigeye snapper (BS‐SP), and yellow croaker (YC‐SP) showed 80% to 92% trypsin inhibitory activity. Trypsin inhibitory activity staining gel electrophoresis revealed bands at 32, 33, 37, 45, 48, and 50 kDa for the 3 species, and a band at 95 kDa was observed for TB‐SP and YC‐SP. Alpha‐1‐antitrypsin with molecular mass of 45 to 50 kDa was identified in YC‐SP by gel‐based liquid chromatography‐tandem mass spectrometry (GeLC‐MS/MS). Other major protein bands appeared on trypsin activity staining included phosphorylase, glyceraldehyde‐3‐phosphate dehydrogenase, and creatine kinase with molecular mass of 95 and 35 to 40 kDa, respectively. But, these 3 proteins did not show true trypsin inhibitory activity. Trypsin inhibitory activity of fractionated sarcoplasmic proteins showed good stability, with >80% activity retained at 60 °C and up to 0.6 M NaCl. TB‐SP showed the highest inhibitory activity against autolysis of washed threadfin bream mince at 65 °C. Addition of 0.5% or 1% TB‐SP improved textural properties of threadfin bream surimi gels preincubated at 37 or 65 °C followed by heating at 90 °C. Therefore, TB‐SP could be a promising protein ingredient for enhancing surimi gel texture.     

Relationship between proteolytic changes and tenderness in prerigor lactic acid marinated beef

A meat tenderising procedure involving injection of a lactic acid solution into prerigor muscle was investigated using beef M pectoralis profundus. The distribution of lysosomal enzymes in subcellular fractions, densities of myofibrillar protein bands after SDS‐PAGE and shear force were measured in non‐injected, 0.5 M and 1.0 M lactic‐acid‐injected samples during a 21 days ageing period. The activities of cathepsin B + L and β‐glucuronidase in the soluble fraction increased with level of lactic acid and with time post‐mortem (P < 0.001). Lactic acid and storage decreased densities of SDS‐PAGE bands migrating at the position of myosin heavy chain (MHC) and α‐actinin and increased densities of a 150 kDa band (P < 0.01). SDS‐PAGE of isolated perimysium cleaved with CNBr showed proteolytic cleavage of collagen after prolonged storage. Lactic acid injection significantly reduced shear force (P < 0.001). The cathepsin B + L activity in the soluble fraction correlated to shear force (r = −0.8), the degradation of MHC and α‐actinin (r = −0.88 and −0.90) and the generation of the 150 kDa fragment (r = 0.90) but not to the generation of a 31 kDa fragment (r = 0.05). A major part of the tenderness improvement after lactic acid injection was complete at 24 h post‐mortem, and was therefore due to a rapid process, eg pH‐induced swelling of the muscle structure. The data on enzyme activities and protein degradation, however, suggested that the action of lysosomal cathepsins also contributed to textural changes. © 1999 Society of Chemical Industry     

Structural and Functional Properties of Hemp Seed Protein Products

The effects of pH and protein concentration on some structural and functional properties of hemp seed protein isolate (HPI, 84.15% protein content) and defatted hemp seed protein meal (HPM, 44.32% protein content) were determined. The HPI had minimum protein solubility (PS) at pH 4.0, which increased as pH was decreased or increased. In contrast, the HPM had minimum PS at pH 3.0, which increased at higher pH values. Gel electrophoresis showed that some of the high molecular weight proteins (>45 kDa) present in HPM were not well extracted by the alkali and were absent or present in low ratio in the HPI polypeptide profile. The amino acid composition showed that the isolation process increased the Arg/Lys ratio of HPI (5.52%) when compared to HPM (3.35%). Intrinsic fluorescence and circular dichroism data indicate that the HPI proteins had a well‐defined structure at pH 3.0, which was lost as pH value increased. The differences in structural conformation of HPI at different pH values were reflected as better foaming capacity at pH 3.0 when compared to pH 5.0, 7.0, and 9.0. At 10 and 25 mg/mL protein concentrations, emulsions formed by the HPM had smaller oil droplet sizes (higher quality), when compared to the HPI‐formed emulsions. In contrast at 50 mg/mL protein concentration, the HPI‐formed emulsions had smaller oil droplet sizes (except at pH 3.0). We conclude that the functional properties of hemp seed protein products are dependent on structural conformations as well as protein concentration and pH.     

Relationship between protein characteristics and film‐forming properties of kidney bean,field pea and amaranth protein isolates

This study was undertaken to evaluate physicochemical (colour, protein content, ash content and zeta potential), structural (size exclusion chromatography and thermal properties) and film‐forming properties of kidney bean, field pea and amaranth protein isolates (KBPI, FPPI and AMPI, respectively). Protein content, ash content, zeta potential and denaturation temperature of the isolates ranged from 83.9 to 91.4%, 2.9 to 4.5%, ?37.3 to ?44.2 mV and 85.5 to 96.2 °C, respectively. Size exclusion chromatography revealed that globulins were prominent proteins in KBPI and FPPI, while AMPI contained both globulins and albumins as major fractions. FPPI showed the highest L* value (88.1), surface charge (zeta potential = –44.2 mV) and protein solubility (80.0–94.2%). Films were prepared from heated (90 °C for 20 min) and unheated protein dispersions of pH 7.0, 8.0 and 9.0 and evaluated for colour, opacity, tensile strength (TS), water‐solubilised matter (WSM) and water vapour permeability (WVP). FPPI films showed the most desirable properties in terms of the highest L* (87.5–90.5), TS (12.6–37.2 MPa) and the lowest opacity (7.1–8.4 A₆₀₀/mm). FT‐IR spectroscopic analysis of the films revealed that alkaline pH and heat treatment unfolded protein molecules. Alkaline pH reduced opacity, while heat treatment improved TS and water resistance (decreased WSM and WVP) of protein films, which varied with the protein isolates.     

Influence of extraction methods on functional properties of protein concentrates prepared from South African bambara groundnut landraces

Functional properties of protein concentrates prepared from three bambara groundnut landraces using acid precipitation and salt solubilisation methods were evaluated. The protein content of bambara grains (26–27%) was similar for the three landraces. The acid precipitation gave a much higher yield of protein concentrates (52%), which were also high in protein (79%) compared to the salt solubilisation method (yield: 25%, protein content: 57%). Functional properties of proteins were more influenced by the methods of preparation rather than the landraces. Protein concentrate prepared by salt solubilisation method showed higher emulsifying (63–66%), foaming (53–57%), water (1.4–2.0 mg mL^?1) and oil absorption properties (2.2–2.6 mg mL^?1) than the acid‐precipitated concentrates (53–57%, 63–66%, 2.0–2.7 mg mL^?1, 1.4–1.7 mg mL^?1). The foaming capacity and stability of all the protein concentrates decreased with increasing pH from 3 to 8. Salt solubilisation may be the most appropriate method for the enhanced functionality and utilisation of bambara groundnuts’ protein concentrates.     

Pea protein exhibits a novel Pickering stabilization for oil-in-water emulsions at pH 3.0

In this paper we reported that pea protein isolate (PPI) at pH 3.0 exhibits a novel Pickering stabilization for oil-in-water emulsions. At pH 3.0, most of the proteins in PPI were present in the nanoparticle form, with the hydrodynamic diameter of 134–165 nm depending on the concentration (c; 0.25–3.0 g/100 mL). For the emulsions formed at a specific oil fraction of 0.2, increasing the c from 0.25 to 3.0 g/100 mL resulted in a considerable reduction in the emulsion size, while their creaming stability progressively increased, and especially at c values higher than 2 g/100 mL, no creaming occurred even after storage of 20 days. Confocal laser scanning microscopy observations showed that increasing the c resulted in a progressive increase in extent of droplet flocculation, and at higher c values, a network consisting of flocculated droplets could be formed. The emulsions formed at c values above 1.0 g/100 mL exhibited extraordinary stability against coalescence. The flocculated droplet network formation was closely associated with the increased amount of adsorbed proteins at the interface. The results suggest that pea proteins exhibit a good potential to act as a kind of Pickering stabilizers for oil-in-water emulsions at acidic pHs.     

Influence of enzymatic hydrolysis,pH and storage temperature on the emulsifying properties of canola protein isolate and hydrolysates

The aim of this work was to enhance emulsification properties of canola proteins through enzymatic proteolysis and pH variaton. Canola protein isolate (CPI) and hydrolysates (CPHs) were used to form emulsions at pH 4.0, 7.0 and 9.0 followed by storage at 4 or 25 °C for 7 days. Controlled enzymatic hydrolysis led to increased peptide bond cleavage with time (0.23 g/100 g in CPI to 7.18 g/100 g after 24‐h Alcalase hydrolysis). Generally, oil droplet sizes were smaller for emulsions made at pH 9.0, which suggest better quality than those made at pH 4.0 and 7.0. Trypsin hydrolysate emulsions were the most physically stable at pH 7.0 and 9.0; in contrast, the pepsin hydrolysate emulsions were unstable at all conditions. The results suggest that selective enzymatic hydrolysis could play an important role in enhancing successful incorporation of canola proteins and peptides into food systems as protein emulsifiers.     

ISOLATION AND CHARACTERIZATION OF TRYPSIN INHIBITORS FROM SOME THAI LEGUME SEEDS

Trypsin inhibitors from cultivars of cowpea (Vigna unguiculata (L.) Wasp.), pigeon pea (Cajanus cajan (L.) Millsp.) and bambara groundnuts (Voandzeia subterranea (L.) Thou) grown in Thailand were isolated and characterized. Extraction of seeds with NaCl rendered a higher recovery of trypsin inhibitor than other solvents tested (P<0.05). The extraction time affected the inhibitor recovery (P<0.05). The extraction time of 3 h was optimum for the recovery of trypsin inhibitor from pigeon and bambara groundnuts, whereas 1 h was optimum for cowpea. Based cn inhibitor activity of zones separated by electrophoresis, the molecular mass of the inhibitor from bambara groundnuts was 13 kDa. Two inhibitory bands were observed for cowpea (10 and 18 kDa) and pigeon pea (15 and 25 kDa). Partial purification of inhibitors was achieved by heat‐treatment at 90C for 10 min, followed by ammonium sulfate precipitation with 30–65% saturation. The partially purified inhibitors from four seeds were heat stable up to 30 min at 90C at pH 7.0. The activities were also retained over a wide pH range at 25C but were lost when samples were treated with β‐mercaptoethanol prior to electrophoresis.     

Effect of thermal treatment on the proteins of amaranth isolates

The effect of thermal treatment of proteins from Amaranthus hypochondriacus was studied. Two protein isolates were obtained from the defatted flour by water extraction at a pH of 9 (A9 isolate) and 11 (A11 isolate), followed by isoelectric precipitation at a pH of 5. Effect of thermal treatment (70 and 90 °C, during 3, 5, 10, 15 and 30 min) on A9 and A11 dispersions were analyzed by differential scanning calorimetry (DSC), polyacrylamide gel electrophoresis, UV spectrophotometry, superficial hydrophobicity and solubility in water. Thermal treatment induced the aggregate formation of high molecular mass stabilized by disulfide and non‐covalent bond. Thermal treatment at 70 °C produced a 30% denaturation in both, while at 90 °C A9 was more denatured than A11 (75% and 55% of denaturation, respectively). An increase in thermal stability was also detected by DSC in A9 treated at 90 °C. The denaturation process was accompanied at short heating times by an increase in UV absorbance and changes in superficial hydrophobicity. A decrease in water solubility (35–50%, depending on time–temperature conditions) was also observed for the A9 isolates. The results suggest that the A9 isolates, enriched in a globulin protein fraction, are more sensitive to thermal treatment than isolates A11 enriched in glutelin protein fraction. The changes shown by both isolates, indeed, could affect their functional properties and could definitely limit their use in food products. Copyright © 2007 Society of Chemical Industry     

Process optimisation and physicochemical characterisation of enzymatic hydrolysates of proteins from co‐products of Atlantic Salmon (Salmo salar) and Yellowtail Kingfish (Seriola lalandi)

The aim of this study was to develop an enzymatic hydrolysis process of protein co‐products for two major commercial fish species in Australia: Atlantic salmon (AS) and Yellowtail kingfish (YTK). The outcomes are to produce high protein recovery of fish protein hydrolysates within controlled molecular weight ranges that display enhanced physicochemical properties of oil binding and emulsification. Three enzymes (Flavourzyme, Neutrase and Alcalase) were applied to processing co‐products. Protein recovery and physicochemical properties were evaluated with increasing hydrolysis time from 30 min to 180 min and ratio of enzyme to substrate (E/S) from 0.5% to 3.0%. In order to achieve a product with optimum emulsifying capacity (50 ± 0.6 m² g^?1), an E/S ratio of 0.6–1.3% Flavourzyme was applied for 30–111 min with a protein recovery of 55%; in order to achieve a product with optimum oil‐binding capacity (8.3 ± 0.3 g oil g hydrolysates^?1), an E/S ratio of 2.3–3.0% Flavourzyme was applied for 25–64 min with a protein recovery of 70%. YTK protein hydrolysates were further membrane‐fractionated into five fractions (>100 kDa, 50–100 kDa, 30–50 kDa, 10–30 kDa and <10 kDa), and of these, the 10–30 kDa exhibited the best properties of oil binding (19 ± 0.3 g oil g hydrolysates^?1) and emulsification (57 ± 0.7 m² g^?1). These results demonstrate the importance of enzymatic hydrolysis of seafood co‐products into high‐value ingredients for food products and processing.     

Influence of pH Shift on Functional Properties of Protein Isolated of Tilapia (<Emphasis Type="Italic">Oreochromis niloticus</Emphasis>) Muscles and of Soy Protein Isolate

The physicofunctional and chemical properties of acid-aided protein isolate (AcPi), alkaline-aided protein isolate (AlPi) and soy protein isolate (SPI) prepared from tilapia muscle and defatted soy flour as a function of pH and/or NaCl concentration were investigated. Both acid- and alkali-aided processes lead to significant recoveries (P < 0.05) of proteins with substantial reduction of lipids in AlPi (0.81%) and AcPi (0.96%), the lowest for SPI (0.336%) facilitated by the processing method and sample used. There is greater lipid reduction at alkali pH, effective removal of impurities such as bones and scales, indicated by percentage ash (AcPi, 4.53%; AlPi, 3.75% and SPI, 3.51%). No major difference noted in sodium dodecyl sulphate polyacrylamide gel electrophoresis protein bands (14.4–97.4 kDa) possibly representing partial hydrolysis of myosin. Solubility was the highest at pH 3.0 and 11.0 and the lowest at isoelectric point with foam capacity showing similarity at varying pH. The addition of NaCl improved foam stability, possibly due to the increased solubility and surface activity of the soluble protein. On the whole, AcPi, AlPi and SPI manifested lower solubility and foamability at pH 4.0 and 5.0. AlPi exhibited appreciable levels of solubility, emulsion capacity, oil-holding capacity, viscosity and whiteness, whereas SPI had appreciable water-holding capacity. AcPi, AlPi and SPI have excellent relevance for product development based on their functionality.     

The postmortem μ‐calpain activity,protein degradation and tenderness of sheep meat from Duolang and Hu breeds

This study aimed to investigate the differences in meat tenderisation between two Chinese native sheep breeds, Duolang and Hu. The tenderness of longissimus thoracis (LT) muscle, μ‐calpain autolysis and proteolysis of myofibrillar protein was measured at 1‐ and 7‐days postmortem storage at 4 °C. At 7‐days postmortem ageing, meat from Duolang sheep was more tender compared to that from Hu sheep. The Warner–Bratzler shear force of Duolang and Hu sheep was reduced by 55.20% and 41.51% at 7 days compared with 1 day, respectively. In Duolang LT, a higher proportion of 80‐kDa μ‐calpain was autolyzed than in the Hu samples at 1‐day postmortem ageing, but they did not differ significantly at 7 days. More titin, desmin and troponin‐T were degraded in Duolang sheep compared to Hu sheep. Additionally, pH values at the different ageing time were not significantly different, indicating that pH may be not a determinant factor contributing to the tenderness difference between the two breeds. Our data suggest the earlier activation of μ‐calpain and a larger extent of proteolysis of key structural proteins may contribute to the higher rate of tenderisation of Duolang compared to Hu sheep during postmortem ageing.     

Presence of lactoferrin in a bovine skim milk fraction with acid phosphatase activity

The aim of this study was to determine the principal active molecules in the acid phosphatase (AcP) fraction of skim milk origin using immunostaining and AcP staining. The AcP fraction was separated from skim milk at 0.38 m NaCl using carboxymethyl cellulose chromatography at pH 5.2. The molecular mass of the active molecule in AcP fraction was estimated to be 80 kDa by immunostaining and AcP staining. The 80 kDa protein was analyzed by a protein sequencer, using the automated Edman degradation method; the first thirteen N-terminal amino acid sequence obtained were shown to be APRKNVRWXTIXQ. For that amino acid sequence, there was 84% (11/13 residues) homology with the amino acid sequence of bovine lactoferrin (LF). The AcP fraction and commercial LF showed a similar AcP activity profile, having an optimum pH of 4.5 and temperature of 60 °C. Thus, the AcP fraction from bovine skim milk was isolated and the principal active molecule present was tentatively identified as LF.     

Effects of temperature,pH and light on the stability of aloin A and characterisation of its major degradation products

This study explored the stability and degradation products of aloin A under varying pH, temperature and light conditions usually encountered in processing. The stability of aloin A was significantly affected by temperature and pH. The content of aloin A decreased by more than 90% within 12 h at 50 °C and within 6 h at 70 °C, respectively. A significant decrease in stability was also observed at higher pHs. At pH 8.0, less than 2% of aloin A remained within 12 h. However, aloin A exhibited good stability at acidic pH levels with 94% remaining at pH 2.0 for 14 days. Light exerted no influence on the stability during the experimental period (14 days). Aloe‐emodin, elgonica‐dimers A and B were characterised as major degradation products of aloin A at pH 5.0 or below, and elgonica‐dimers were mainly formed at 4 °C as well. 10‐hydroxyaloins A and B were found under any condition except at pH 2.0 and 3.0, and they were mainly formed under high temperature, neutral‐basic and any light conditions.     

New processing of lupin protein isolates and functional properties

A growing demand for functional plant proteins could be identified, which properties are customized for specific applications and formulations as food ingredients. Native lupin proteins (α, β, γ) conglutin have a good solubility at appropriately chosen conditions. A novel procedure has been proposed to maintain the native protein properties. Lupin proteins are extracted from hexane deoiled lupin. The protein product type E comprises high molecular weight proteins (α, β‐conglutin( which are separated using alkaline extraction and acid precipitation procedures. The protein product type F is enriched in the γ‐conglutin fraction and is separated from the acid pre‐extract applying cross flow filtration at pH 7–8. For the zirconium oxide membrane the filtration rate can be increased by appropriately chosen pH conditions up to 70 l/m²h. Lupin protein fraction (type E and F) are highly soluble protein isolates with outstanding emulsification, salt tolerance and foaming properties. These new lupin proteins (type E and F) offer extremely interesting properties for application in food systems and are available from pilot plant fractionation.     

Emulsifying properties of proteins extracted from Australian canola meal

Canola protein albumin fraction, globulin fraction, and canola protein isolate (CPI) were compared to commercial soy protein isolate (SPI) in terms of their emulsifying properties at various pH values. The globulin fraction had higher emulsifying capacity (EC), higher emulsifying activity index (EAI), and the droplet size of emulsions it stabilized was consistently smaller irrespective of pH compared to albumin fraction or CPI. In comparison to SPI, globulin fractions also had higher EC at all pH values tested, higher EAI at acidic pH, and smaller or comparable average emulsion droplet size at both pH 4 and 7. The stability of canola protein based emulsions were comparable to those of SPI based emulsions at most pH values (except the emulsion stabilized by the CPI at pH 4), with no significant (p > 0.05) changes in droplet size during storage for up to 7 days at room temperature. These emulsions, however, experienced separation into the emulsion and serum phases after 24 h storage at room temperature with the exception of CPI- and SPI-stabilized emulsions at pH 9. This study demonstrates the comparable emulsifying properties (forming or stabilizing) of some canola proteins to commercially available SPI, suggesting the potential use of canola proteins in food applications.