Effects of transglutaminase treatment on the thermal properties of soy protein isolates

The effects of covalent cross-linking of microbial transglutaminase (MTGase) on the thermal properties of soy protein isolates (SPI), including the thermal denaturation and glass transition were investigated by conventional and modulated differential scanning calorimetry (DSC). The MTGase treatment significantly increased the thermal denaturation temperatures (including the on-set temperature of denaturation, T_m and the peak temperature of denaturation, T_d) of glycinin and β-conglycinin components of SPI (P ⩽ 0.05), and the thermal pretreatment of SPI further increased the extent of this improvement. The MTGase treatment also improved the ability of SPI to resist the urea-induced denaturation. Modulated DSC analysis showed that there were two glass transition temperatures (T_g) in the reversible heat flow signals of native SPI (about 5% moisture content), approximately corresponding to 45 and 180 °C, respectively. These T_g values of SPI were significantly decreased by the MTGase treatment (at 37 °C for more than 2 h) (P ⩽ 0.05). The improvement in the hydration ability of protein and the formation of high molecular biopolymers may account for the changes of thermal properties of soy proteins caused by the MTGase cross-linking.     

Subunit,amino acid composition and in vitro digestibility of protein isolates from Chinese kabuli and desi chickpea (Cicer arietinum L.) cultivars

The subunit, amino acid composition and in vitro digestibility of the two protein isolates (GCPI and ZCPI) from one kabuli and one desi chickpea cultivars, grown extensively in Xinjiang Autonomous Region of China, were investigated and compared with those of soy protein isolate (SPI). SDS–PAGE showed that GCPI and ZCPI had almost the same band components under the reduced and unreduced conditions, with only minor difference in relative quantity for some bands, but different from that of SPI. The sulphur-containing amino acids were the first limiting amino acids for all three protein isolates of GCPI (2.11 g/100 g), ZCPI (2.20 g/100 g) and SPI (1.99 g/100 g). Amino acid score of the three protein isolates could reach the FAO/WHO requirement (1990) for the essential amino acids for preschool children. The order of in vitro digestibility was GCPI (87.47%) > ZCPI (80.82%) > SPI (71.04%). Our results indicated that, compared with soybean protein isolate, Chinese kabuli and desi chickpea protein isolates had higher digestibility value, and chickpea protein, especially for kabuli protein, could be utilized as a good source of protein for human nutrition.     

Effect of soy protein substitution for sodium caseinate on the transglutaminate-induced cold and thermal gelation of myofibrillar protein

The influence of soy protein isolate (SPI) substitution for sodium caseinate (SC) on the properties of cold-set (4 °C) and heat-induced gels of pork myofibrillar protein (MP) incubated with microbial transglutaminase (TG) was investigated. The strength of cold-set MP–SC gels (formed in 0.45 M, NaCl, 50 mM phosphate buffer, pH 6.25) increased with time of TG incubation, but those gels with more than 66% SPI substituted for SC had a >26% reduced strength (P < 0.05). Upon cooking, both incubated and non-incubated protein sols were quickly transformed into highly elastic gels, showing up to 6000 Pa in storage modulus (G′) at the final temperature (72 °C). However, no differences (P < 0.05) in G′ were observed between heated samples with SPI and SC. Myosin heavy chain, casein and soy proteins gradually disappeared with TG incubation, contributing to MP gel network formation. Both cold-set and heat-induced gels had a compact protein matrix, attributable to protein cross-linking by TG.     

Coating papers with soy protein isolates as inclusion matrix of carvacrol

Antimicrobial papers were prepared by coating paper with soy protein isolate (SPI) solution as inclusion matrix of carvacrol, an antimicrobial agent. Addition of carvacrol (30% w/w of SPI) to SPI solution (10% w/v) prepared at 25 °C induced soy protein aggregates and viscosity decrease. Heat treatment (50, 70, 90 °C) of SPI solutions and carvacrol addition improved homogeneity reduced particles size and increased viscosity of solutions. The aggregated structure of SPI in the presence of carvacrol at 25 °C may play the role of a trapping structure leading to low carvacrol losses during coating and drying process of paper (9.6% against 37% after heat treatment at 90 °C) and to lower release rates specially the first three days (0.04 g/m²/day and 0.31 g/m²/day when SPI coating solutions were prepared at 25 and 90 °C, respectively). Regardless of the heat treatments received by the SPI solutions, residual carvacrol quantities in the coated papers after 50 days ranged between 0.6 and 0.7 g/m².     

Characterization of low-phytate soy protein isolates produced by membrane technologies

Soy protein isolates (SPI) produced by combining electro-acidification and tangential ultrafiltration/diafiltration (UF/DF) (pH 6), were compared in terms of composition and proteins solubility with isolates produced by UF/DF (pH 9) and isoelectric precipitation (pH 4.5). Mineral and phosphorus (phytic acid) removal was enhanced for the SPI pH 6. Whey-like proteins (M.W. < 66 kDa) were also found in higher concentration for the SPI produced by membrane technologies. This difference in composition resulted in improved solubility characteristics for the SPI pH 6 by as high as 25% and 60%, when compared to the SPI pH 4.5 and SPI pH 9, respectively. Improvement in solubility was most important between pH 2 and 4.5. The quantity of H⁺ ions added to the soy protein extract (SPE) and SPI to reduce the pH from 9 to 4.5, during solubility measurement, was related to the degree of proteins aggregation, as determined by size-exclusion high-performance liquid chromatography, and at a lesser extent to their phytic acid content. For the pH range of 4.5 to 2, the degree of proteins aggregation alone determines the quantity of H⁺ ions added.Industrial relevanceSoy protein production is one of the major agricultural sectors of significant importance to North America and soy proteins represent 69% of global plant protein consumption in the world. Soy protein concentrates and isolates are produced at the industrial scale by isoelectric precipitation. This process has a high productivity, however, it also generates large volumes of effluent. The final products also have significant contents of minerals and of phytic acid, the latter of which is well known to decrease the proteins and minerals adsorption in the intestine.We were the first group to combine bipolar membrane electrodialysis (BMED) and ultrafiltration (UF) (dead-end) for the production of soy protein concentrates (Mondor, Ippersiel, Lamarche & Boye, 2004). The new approach resulted in a significant decrease of the volumes of effluent due to the use of BMED to adjust the pH of the extract prior to UF and by improving the protein washing step using diafiltration (DF). It was also shown that for the pH range 6–9, minerals and phytic acid removal was improved with a decrease in pH. In this work, we present the characteristics of a soy protein isolate with a low phytic acid/protein ratio (SPI pH 6) produced by BMED and tangential flow UF/DF applying an optimal VCR5, re-VCR 5 sequence at pH 6. The SPI pH 6 shows an improved solubility by as high as 25% and 60%, when compared to an isolate produced by isoelectric precipitation at pH 4.5 and to one produced by UF/DF at pH 9, respectively. Improvement in solubility was most important between pH 2 and 4.5 indicating that this isolate could be considered as a valuable ingredient for the formulation of fruit juice beverages or power juices, considering that the pH of these liquid food products is around 3.5.     

Effect of processing parameters on the properties of transglutaminase-treated soy protein isolate films

The effects of processing parameters, including the applied amount of microbial transglutaminase (MTGase), the pH of film-forming solution, air-drying temperature, as well as the additional pre-incubation, on the properties of MTGase-treated soy protein isolate (SPI) films were investigated. The treatment with low concentration of MTGase (4–10 units per gram of SPI, U g^− 1) significantly increased the tensile strength (TS) values of SPI films, while high concentration of MTGase (over 20 U g^− 1) resulted in significant decrease in the TS values (P ≤ 0.05). The elongation at break (EB) values of corresponding films gradually decreased, and the contact angle values persistently increased with the enzyme concentration. At alkaline pH range, the TS and EB values of MTGase-treated SPI films were significantly higher than that at pH 7.0 (P ≤ 0.05). Meanwhile, the contact angle values significantly decreased with increasing pH from 7.0 to 10.0 (P ≤ 0.05). The TS, EB and contact angle values of MTGase-treated films gradually but insignificantly decreased with increasing the air-drying temperature from 18 to 50 °C (P > 0.05). The properties of MTGase-treated films were also affected by the additional pre-incubation of film-forming solutions with MTGase before casting. Furthermore, the aggregation of SPI or its components induced by MTGase has been proved to mainly account for the influence of processing parameters on the properties of SPI films (MTGase-treated). Thus, low concentration of enzyme, alkaline pH range and low air-drying temperature, at which conditions the MTGase-induced aggregation of SPI in film-forming solutions could be in some extent inhibited or delayed, might facilitate the improvement of the properties of SPI films by MTGase, especially the mechanical and surface hydrophobic properties.Industrial relevanceThe development of biodegradable protein film has attracted a lot of attention worldwide. The enzymatic cross-linking induced by transglutaminase has been confirmed to improve mechanical and surface hydrophobic properties of cast films from most of food proteins, including soy proteins. Results of this study show that, the improvement of properties of cast films of soy proteins by transglutaminase treatment is largely dependent upon many processing parameters, e.g., enzyme concentration, the pH of film-forming solution and temperature.     

Effects of flaxseed oil concentration on the performance of a soy protein isolate-based emulsion-type film

Biodegradable edible films have the potential to either replace or reduce the amount of synthetic packaging utilized by the food industry. The overall goal of this research was to investigate the effect of flax seed oil concentration (1–10%) on the mechanical, moisture barrier and swelling properties of soy protein isolate (SPI) (5.0% w/w SPI, 40% w/w glycerol) emulsion-based films. Film forming solutions showed a bimodal oil droplet distribution with peak sizes occurring at < 10 and ~ 100 μm. As the oil content increased, the size distribution shifted towards smaller droplet sizes. An equal size ratio was noted at the 5.0% oil content level. All film forming solutions were pseudoplastic in nature, where viscosity increased from 18 to 58 mPa (at 1 s^− 1) as a function of oil content (3% to 10%). Tensile strength of formed films reached a maximum at 5.35 MPa at the 5% w/w oil level, whereas tensile elongation increased from 11.3% to 22.2% with increasing oil content. Puncture strength and deformation, as well as water vapour permeability was relatively independent of the oil content. Moisture content and swelling properties of formed films were found to both decrease from 22.8% to 18.7%, and from 3114% to 1209%, respectively as the oil content was raised from 1 to 10%, and films became darker, redder and more yellow in colour as the percentage of flax seed oil increased.     

Ultra-High Pressure Homogenization enhances physicochemical properties of soy protein isolate-stabilized emulsions

The effect of Ultra-High Pressure Homogenization (UHPH, 100–300 MPa) on the physicochemical properties of oil-in-water emulsions prepared with 4.0% (w/v) of soy protein isolate (SPI) and soybean oil (10 and 20%, v/v) was studied and compared to emulsions treated by conventional homogenization (CH, 15 MPa). CH emulsions were prepared with non-heated and heated (95 °C for 15 min) SPI dispersions. Emulsions were characterized by particle size determination with laser diffraction, rheological properties using a rotational rheometer by applying measurements of flow curve and by transmission electron microscopy. The variation on particle size and creaming was assessed by Turbiscan® analysis, and visual observation of the emulsions was also carried out. UHPH emulsions showed much smaller d_3.2 values and greater physical stability than CH emulsions. The thermal treatment of SPI prior CH process did not improve physical stability properties. In addition, emulsions containing 20% of oil exhibited greater physical stability compared to emulsions containing 10% of oil. Particularly, UHPH emulsions treated at 100 and 200 MPa with 20% of oil were the most stable due to low particle size values (d_3.2 and Span), greater viscosity and partial protein denaturation. These results address the physical stability improvement of protein isolate-stabilized emulsions by using the emerging UHPH technology.     

Tracking isoflavones: From soybean to soy flour,soy protein isolates to functional soy bread

Soybean seeds with three different levels (low, intermediate and high) of isoflavones were processed to soy flour and soy protein isolates (SPIs) and developed into functional soy breads. The effect of factors involved in all steps of the process was investigated by tracking the composition and concentration of native forms of isoflavones. The total isoflavone contents were 8033.3, 10570.1 and 15169.0 nmol/g DM (dry matter) in the three soybeans; 13201.5, 20034.4 and 26014.3 nmol/g DM in defatted soy flours; 9113.2, 13274.6 and 17918.3 nmol/g DM in the SPI; 2782.7, 4081.4 and 5590.3 nmol/g DM in soy breads, respectively. The bread making processes did not affect the total isoflavone content, but changed glucosides/acetylglucosides to aglycones. Malonylglucosides were stable prior to baking but degraded to acetylglucosides and further to glucosides during baking. Our results provide critical information for the production of functional soy breads that contain varying amounts of soy isoflavones.     

The effect of pH on the gelling behaviour of canola and soy protein isolates

The present study investigates the gelation mechanisms of a canola protein isolate (CPI) as a function of a pH (3.0–9.0), and compares it to that of a commercial soy protein isolate (SPI). A rheological investigation found that CPI was non-gelling at pH 3.0, and then formed a gel with increasing strength as pH was raised from pH 5.0 to 9.0. In contrast, the commercial SPI ingredient was found to be non-gelling at pH 9.0, but formed the strongest networks at pH 5.0 near its isoelectric point (pI = 4.6). Denaturation temperature as determined by differential scanning calorimetry were found to occur at ~ 78 °C for CPI at pH 5.0, then shifted to higher temperatures (~ 87 °C) at pH 7.0/9.0, whereas detection of SPI denaturation could not be obtained due to instrument sensitivity. Gelling temperatures were similar for both CPI and SPI (~ 82–86 °C) at all pHs, with the exception of SPI at pH 5.0 (~ 46 °C). Overall CPI networks were stronger than SPI, since the latter had weaker inter- and intramolecular junction zones. Confocal laser scanning microscopy images indicated that CPI gels became denser with lower lacunarity values as pH increased from 3.0 to 9.0. Moreover, the fractal dimension of CPI gels was found to increase from ~ 1.5-1.6 to ~ 1.8 as pH increased from 5.0/7.0 to 9.0, respectively suggesting diffusion-limited cluster-cluster aggregation. Images of SPI networks were not concurrent with fractal analysis under the conditions examined. Despite CPI having excellent gelling properties that are comparable to SPI, its need for alkaline pH conditions will limit its applicability in foods.     

Gelling of microbial transglutaminase cross-linked soy protein in the presence of ribose and sucrose

Soy protein isolate (SPI) was incubated with microbial transglutaminase (MTGase) enzyme for 5 (SPI/MTG(5)) or 24 (SPI/MTG(24)) h at 40 °C and the cross-linked SPI obtained was freeze-dried, and heated with 2% (w/v) ribose (R) for 2 h at 95 °C to produce combined-treated gels. Longer incubation period resulted in more compact and less swollen SPI particle shape when reconstituted with sugar solution. Thus, this MTGase treatment affected samples in terms of flow behaviour and gelling capacity. Rheological study showed different gelling profiles with the cross-linking treatments and combined cross-linked SPI gave a higher G′ value compared to single treated samples. These are due to the formation of additional ε-(γ-glutamyl)lysine bonds and “Maillard cross-links” within the SPI protein network during the MTGase incubation and heating in the presence of ribose (i.e. reducing sugar). Network/non-network protein analysis found that network protein increased with cross-linking treatment, which also resulted in different SDS–PAGE profiles. As in non-network protein fraction, A₄ subunit was suggested to become part of the network protein as a result of combined cross-linking.     

Physicochemical and functional properties of soy protein isolate as a function of water activity and storage

The effect of storage temperature on the physicochemical characteristics, solubility and gelling properties of soy protein isolate (SPI) with different water activities (a_w) was investigated. SPI with a_w of 0.19 (SPI-0.19) was placed in environments with relative humidity (RH) of 33% and 74%. After reaching equilibrium, in 20 days, the samples were named SPI-0.33 and SPI-0.74. For SPI-0.74, modifications in the protein characteristics started during the equilibrium period, with a decrease in the solubility and alterations in both the electrophoretic profile of the soluble proteins and in the gelling characteristics. During the 180-day storage period, SPI-0.19 and SPI-0.33 showed similar behaviours: decrease in protein solubility and alteration in hardness, cohesiveness and microstructure of the gels. These alterations were more pronounced during storage at 45 °C than at 25 °C, and in SPI-0.33 more than in SPI-0.19. Results suggest that storage conditions – temperature and RH – affect the functional properties of the proteins and the use of the isolates as a functional ingredient.     

Quercetagetin loaded in soy protein isolate–κ-carrageenan complex: Fabrication mechanism and protective effect

In the present study, the potential of soy protein isolate (SPI)–κ-carrageenan (κ-CG) complex as a protective carrier for quercetagetin was investigated at different pH values (pH 2.3 and 6.5). The particle size of the ternary aggregates was slightly increased at pH 2.3, yet dramatically decreased at pH 6.5 with increasing quercetagetin concentration. Moreover, the negative ζ-potential of the ternary aggregates was increased significantly (p < 0.05) at pH 6.5. The addition of quercetagetin to the SPI–κ-CG complex could highly quench the intrinsic fluorescence of SPI. Circular dichroism spectra further suggested that the bound quercetagetin could induce the rise of β-sheet and β-turn contents at the cost of α-helix and unordered coil fractions of SPI. In addition, quercetagetin could increase the viscoelasticity of the ternary aggregates at both pH. Furthermore, the SPI–κ-CG complex was found to be superior to single SPI or κ-CG in terms of improving light stability and radical scavenging ability of quercetagetin.     

Formation and properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase

The gelation and gel properties of glycinin-rich and β-conglycinin-rich soy protein isolates (SPIs) induced by microbial transglutaminase (MTGase) were investigated. At the same enzyme and protein substrate concentrations, the on-set of gelation of native SPI and the viscoelasticity development of correspondingly formed gels depended upon the relative ratio of glycinin to β-conglycinin. The turbidity analysis showed that the glycinin components also contributed to the increase in the turbidity of SPI solutions incubated with MTGase (at 37 °C). Textural profile analysis indicated that the glycinin components of SPIs principally contributed to the hardness, fracturability, gumminess and chewiness values of corresponding gels, while the cohesiveness and springness were mainly associated with the β-conglycinin components. The strength of MTGase-induced gels of various kinds of SPIs could be significantly improved by the thermal treatment. The protein solubility analyses of MTGase-induced gels, indicated that besides the covalent cross-links, hydrophobic and H-bondings and disulfide bonds were involved in the formation and maintenance of the glycinin-rich SPI gels, while in β-conglycinin-rich SPI case, the hydrophobic and H-bondings were the principal forces responsible for the maintenance of the gel structure. The results suggested that various kinds of SPI gels with different properties could be induced by MTGase, through controlling the glycinin to β-conglycinin ratio.     

Protein and glycerol contents affect physico-chemical properties of soy protein isolate-based edible films

This study was conducted to determine the effect of both soy protein and glycerol contents on physico-chemical properties of soy protein isolate-based edible (SPI) films. The aim of this study was to better understand the influence of SPI and GLY contents on the behavior of the physico-chemical properties of soy protein isolate-based films. Films were casted from heated (70 °C for 20 min) alkaline (pH 10) aqueous solutions of SPI at 6, 7, 8, and 9 (w/w %), glycerol (50%, w/w, of SPI) and SPI at 7 (w/w %), glycerol (40, 60, 70 %, w/w of SPI). Water vapor permeability (WVP), was measured at 25 °C and for four different relative humidities (30–100%, 30–84%, 30–75%, 30–53%). Surface properties and differential scanning calorimetry were also measured. Varying the proportion of SPI and GLY had an effect on water vapor permeability, wetting and thermal properties of SPI films. A synergistic effect of glycerol and protein was observed on the water vapor permeability. Glycerol and RH gradient strongly enhance the moisture absorption rates and permeability of SPI based films. SPI content weakly increases the WVP and does not modify the surface properties. The temperature of denaturation of soy protein decreases glycerol content except for the higher concentration whereas it increases with protein ratio.Industrial relevanceThis topic of research aims to control mass transfers within composite foods or betweenfoods and surrounding media (for instance the headspace in packagings). The targeted applications from this work deals with the food product coating or the coating of paper-based packaging for limiting both the loss of water and flavors by cheese based products. This will allow to maintain the weight of the cheese during “ripening” and commercialization, and also to prevent (off-) flavour dissemination from very odorant cheese as produced in France and Poland.     

Preparation of hypocholesterol peptides from soy protein and their hypocholesterolemic effect in mice

The yield and in vitro hypocholesterolemic activity of low-molecular weight soy protein hydrolysates were studied. The yield and cholesterol micellar solubility inhibitory rate (CMSIR) were higher for soy protein Alcalase hydrolysates (SAPH) than soy protein AS1398 hydrolysates (SNPH). The highest CMSIR of 48.6% was found with SAPH with a degree of hydrolysis (DH) of 18%. Optimal parameters for desalting SAPH with macroporous adsorption resin DA201-C were decided to be pH 4.5, SAPH dispersion to resin ration 75:100, and a loading rate 1 BV/h, at which the adsorption rate of the peptide was 89.7%. Only a 4% decrease in CMSIR was found with SPAH (DH 18%) after gastrointestinal protease digestion. In a mice feeding study for 30 d, the serum level of LDL-C + VLDL-C in the SAPH diet group with 0.5 and 2.5 g/kg BW SAPH decreased by 34% and 45% respectively compared to the mice fed only the hypercholesterolemia diet.     

High-pressure treatment effects on proteins in soy milk

Effects of high-pressure treatment on the modifications of soy protein in soy milk were studied using various analytical techniques. Blue shifts of λ_max could be observed in the fluorescence spectra. Spectrofluorimetry revealed that the soy protein exhibited more hydrophobic regions after high-pressure treatment. Electrophoretic analysis showed the change of soy protein clearly and indicated that soy proteins were dissociated by high pressure into subunits, some of which associated to aggregate and became insoluble. High-pressure denaturation occurred at 300 MPa for β-conglycinin (7S) and at 400 MPa for glycinin (11S) in soy milk. High pressure-induced tofu gels could be formed that had gel strength and a cross-linked network microstructure. This provided a new way to process soy milk for making tofu gels.     

Physicochemical and emulsifying properties of protein extracted from soybean meal assisted by steam flash-explosion

The conventional alkaline aqueous extraction is not effective in promoting maximum protein yield from soybean meal (SBM). In this study, the steam flash-explosion (SFE) treatment was firstly employed to significantly improve the protein yield, while the protein content of soy protein isolate (SPI) decreased, concomitant with increase in carbon content of SPI. The SFE treatment led to the dissociation of insoluble protein aggregates in SBM, with subsequent increase of soluble protein aggregates formed via on-disulfide covalent bonds. The covalent coupling of the carbohydrate to the protein during SFE treatment can contribute to the dissolubility of protein and the formation of protein aggregates. After SFE treatment, surface hydrophobicity of SPI was decreased, however the emulsifying properties were improved. The emulsifying activity index and emulsifying stability index were improved to 41.94 m²/g and 35.27 min under 1.3 MPa, 180 s treatment condition. It indicated that compared to surface hydrophobicity, changes of other aspects of protein structure including the covalent coupling of carbohydrate to protein were the predominant factors that ruled the emulsifying property of protein.Industrial relevanceThe steam flash-explosion treatment (SFE) is an eco-friendly, low-energy and non-traditional technology, which could be performed on a large scale for the industry. The SFE treatment can effectively change the physicochemical properties of protein resulting in significant increase of protein yield and improvement in emulsifying properties of protein. After SFE treatment, the protein from heat-denatured soybean meal can be refunctionalized for application in food industry.     

Effects of calcium and high pressure on soybean proteins: A calorimetric study

The effects of calcium and high pressure (HP) treatment on the thermal properties of soybean proteins were analyzed in soybean protein isolate (SPI), a β-conglycinin-enriched fraction (7SEF), a glycinin-enriched fraction (11SEF), and whey protein concentrate (WPC). For β-conglycinin, the temperature of denaturation (Td) decreased with up to 12.5 mM or 6.2 mM calcium in SPI and 7SEF, respectively. This parameter increased when calcium was more concentrated. The Td of glycinin increased for every assayed calcium concentration. The values of changes in Td (ΔTd) depended on calcium concentration and the proportion of β-conglycinin and glycinin in the samples. Activation energy decreased for glycinin in the presence of calcium. HP treatment promoted denaturation of β-conglycinin and glycinin. Calcium protected both proteins in SPI, 7SEF and 11SEF at 200 MPa, and protected glycinin in SPI and 7SEF at 400 and 600 MPa. Nevertheless, calcium increased the degree of denaturation of β-conglycinin in 7SEF at 600 MPa. In the absence of calcium, partially-HP-denatured polypeptides exhibited the same or lower Td than controls, whereas in its presence, they exhibited higher Tds than their respective controls.     

Electrospun soy protein isolate-based fiber fortified with anthocyanin-rich red raspberry (Rubus strigosus) extracts

In this study, electrospun soy protein isolate (SPI) nanocomposite fiber mats were developed utilizing the lowest concentration possible of poly(ethylene oxide) (PEO) containing the highest levels of anthocyanin-rich red raspberry (Rubus strigosus) extract [ARRE; 20% raspberry powder in 95% ethyl alcohol/water/85% lactic acid (80:19:1; v/v/v)]. Variations in the physicochemical attributes of SPI nanofiber mats were investigated as a function of adding ARRE before and after protein denaturation. The electrical conductivity of fiber-forming solutions significantly decreased with increasing ARRE. Scanning electron microscopy (SEM) imaging did not reveal noticeable overall microstructural morphological differences (seen as beads-on-fiber structures) but slightly altered the density of beads in the electrospun SPI fibers. Fourier transform infrared (FTIR) spectroscopy provided insights into the hydrogen bonding interactions between ARRE and SPI in relations to the processing methods used. Specifically, the addition of ARRE after denaturation of SPI caused the amide I bond at 1656 cm^− 1 of SPI to dramatically increase, which indicates ARRE induced CO stretching vibration of soy protein, possibly due to the attachment of polyphenols in ARRE to the hydrophobic pockets of the soy protein side-chains. Simultaneously, the addition of ARRE after SPI denaturation imparts fiber forming solutions with a significant higher level of bioactive anthocyanins and a greater antibacterial activity against Staphylococcus epidermidis, this illustrates that anthocyanin-rich plant extracts could serve as new biological ingredients to create novel active/functionalized SPI-based nanomaterial in food systems.