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.     

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.     

Structural and rheological properties of amaranth protein concentrate gels obtained by different processes

The heat-induced gelation of amaranth protein concentrates (APCs) by three processes was studied. The first was the conventional process for isolating protein (standard process-st), the second included an acid washing step prior to protein extraction (acid washing process-aw) and the third included heating (50 °C) during the alkaline extraction step (heat process-ht). The dispersions (12%, w/v) were heated to 55–90 °C and assessed by rheological measurements made under small deformations, whereas the gels obtained by heating at 70, 80 or 90 °C/30 min were subjected to uniaxial compression measurements (TPA and mechanical properties). The rheological parameters associated with the network structure, elasticity modulus (E) and storage modulus (G′), increased with increasing gelation temperature. For the APCst and APCht gels, protein aggregation occurred in two steps, whereas for APCaw, gelation occurred in a single step. The APCht gels showed the highest fracturability, hardness and adhesiveness, followed by the APCst and APCaw gels (p < 0.05). Similar results were obtained for the mechanical properties at fracture. Increasing the heat treatment temperature from 80 to 90 °C resulted in a more structured matrix with greater water-holding capacity as compared to gels obtained at 70 °C, and these properties were influenced by the extraction processes used to obtain the APCs. Heat extraction (APCht) improved the gelation and water-holding properties, whereas the acid treatment had the opposite effect.     

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.     

Assessment of the effects of soy protein isolates with different protein compositions on gluten thermosetting gelation

Although soy proteins are known to have a deleterious effect on gluten thermosetting gelation, the causes are still poorly understood. Different sources of soy protein isolates (SPI) were used to investigate the interactions between gluten and soy proteins during hydro-thermal treatments. Commercial SPI and isolates prepared from soybean lines with different subunit composition were used to study the influence of protein denaturation and subunit composition on thermoset gel formation. Rapid Visco Analyser analysis showed that replacement of gluten with more than 1% SPI decreased the peak viscosity and interfered with formation of thermoset gels. However, peak viscosity was higher for 11% gluten + 2% SPI than for 11% gluten alone, suggesting a cooperative effect. After heating and cooling, 11% gluten + 2% SPI rich in A1 and A2 subunits formed a coherent thermoset gel suggesting that the cysteine residue content of soy proteins can affect gel formation.     

Gelation properties of salt soluble meat protein and soluble wheat protein mixtures

Salt soluble meat proteins (SSMP) and commercially available soluble wheat proteins (SWP) were characterised by SDS-polyacrylamide gel electrophoresis, differential scanning calorimetry (DSC) and small and large deformation testing. DSC scans indicated transitions similar to those of native actomyosin for the salt soluble meat extract whereas SWP did not indicate any transitions between 20 and 120 °C. Small deformation tests on SWP indicated a G′/G″ crossover gelation temperature of 90 °C and weak gels as judged by frequency sweeps. In contrast, SSMP gelled at 40 °C and formed strong gels on heating to 90 °C. However, on autoclaving at 120 °C, 20% SWP in distilled water produced strong elastic gels with little syneresis, compared with the more brittle gels produced with 20% (w/w) SSMP as indicated by large deformation testing. Mixtures of the two proteins in the ratio SSMP/SWP (15:5) gave strong elastic gels similar to the SWP gels. Even the presence of very small amounts of SWP in the mixture, e.g. SSMP/SWP 20:1 trebled the elastic modulus compared with a SSMP gel and reduced syneresis. This was probably due to the close association of SWP with actomyosin strands as viewed by transmission electron microscopy. However, increased levels of SWP in the mixture, for example SSMP/SWP 10:10 ratio, resulted in the separation of the two protein phases as shown by phase contrast microscopy, and consequently led to lower G′ values in the mixed gels. The addition of 20 mM chloride salts showed that potassium reduced the shear modulus, sodium had no effect and calcium enhanced the shear modulus for SWP gels formed at 120 °C. In contrast, SSMP gels were stronger in the presence of potassium, followed by sodium and calcium.     

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.     

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.     

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.     

Effect of preheating temperature and calcium ions on the properties of cold-set soybean protein gel

To elucidate the effect of preheating temperature and calcium ions on the properties of cold-set soybean protein gel, Ca²⁺ induced gelation of soybean protein were investigated by rheological approaches, electrophoresis analysis, confocal scanning laser microscopy (CSLM) and surface hydrophobicity (S₀). The results showed that, both CaCl₂ concentration (20–40 mM) and preheating temperature (80–120 °C) took significant influence on the dynamic viscoelasticity of the gel samples. The bands distribution of samples preheated at 120 °C were different from the bands distribution of samples preheated below 100 °C in denature and native electrophoresis. The CSLM analysis showed that the gel became coarser as the Ca²⁺ increased. On the other hand, two different kinds of gel were shown under the same Ca²⁺ concentration: a bead-like structure (below 100 °C) and a filamentous structure (above 100 °C). According to fractal theory, weak-linked gel (α was >0.8) was formed when preheating below 100 °C, while a transition gel (α = 0.52–0.62) was obtained when preheating over 100 °C. All these results suggested that the preheating temperature influence the type of cold-set gel.     

Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase

Alkali (pH₁₂) and acid (pH_1.5) pH-treated soy protein isolates (SPI) were incorporated (0.25–0.75% protein) into sols of myofibrillar protein (MP, 3%, in 0.6 M NaCl at pH 6.25) with or without 0.1% microbial transglutaminase (TG) to investigate the potential as meat processing ingredients. Static and dynamic rheological measurements showed significant enhancements of MP gelling ability by the inclusion of pH_1.5-treated as well as preheated SPI (90 °C, 3 min). A 7-h incubation with TG accentuated the gel-strengthening effect by these SPI samples. The B subunit in 11S of SPI was the main component manifesting structure reinforcement in the mixed gels. The MP gelling properties were also greatly improved (P < 0.05) by the addition of 10% canola oil emulsions stabilized by pH-treated SPI. The principal force in the MP gels incorporated with pH-treated SPI was hydrophobic patches; in the presence of TG, cross-linking of previously dissociated A and B subunits of 11S was also intimately involved.     

Gelation properties of salt-extracted pea protein induced by heat treatment

Gelation is one of the most important properties of plant proteins. In this paper, a low denaturation salt extraction method was used to extract pea (Pisum sativum L.) protein isolate from commercial pea flour. The gelation properties of this isolate were examined and compared to commercial products. The pea protein isolate followed the three-step process of gelation that is generally accepted for heat-induced gelation of globular proteins. The minimum gelation concentration of salt-extracted pea protein isolate (PPIs) was 5.5% while that of commercial pea protein isolate (PPIc) was 14.5%. The gelling point was in the range of 82–86 °C for 14.5% PPIs, 0.3 M NaCl at natural pH (5.65). With increasing heating rate, the gelling point tended to increase. Higher heating and cooling rates resulted in decreased final G′ (storage modulus) and G″ (loss modulus) values, indicative of decreased gel strength. A higher protein concentration resulted in higher G′ and G″ values and it was found that there was a power law relationship between protein concentration and G′ and G″. Tan delta (δ) values decreased with increasing protein concentration and at concentrations of 5.5% and above, tan δ remained constant which means the critical concentration for gel formation was 5.5%. The values of G′ and G″ for PPIs were greater than those of PPIc, and tan δ of PPIs was smaller, indicative of a stronger gel network. DSC data showed that PPIc had undergone denaturation whereas PPIs had not (ΔH = 15.81 J/g protein). Although rheometer data showed that the final G′ value of commercial soy protein isolate (SPIc) was smaller than that of PPIs, the gel prepared with SPIc was visually stronger than that of PPIs. The rheological data obtained with small amplitude oscillatory testing was not consistent with the actual observations. Overall, the low degree of denaturation of the PPIs resulted in a stronger gel than that of PPIc making the PPIs a more attractive food ingredient.     

Gelation of single heated vs. double heated whey protein isolate

Gelation of single and double heated whey protein dispersions was investigated using Ca²⁺ as inducing agents. Whey protein isolate (WPI) dispersions (10% w/w) were single heated (30 min, 80 °C at pH 7.0) or double heated (30 min, 80 °C at pH 8.0 and 30 min, 80 °C at pH 7.0) and diluted to obtain the desired protein and/or calcium ions concentration (4–9% and 5–30 mm, respectively). Calcium ions were added directly or by using a dialysis method. Double-heated dispersions gelled faster at lower protein and calcium ion concentrations than single-heated dispersions. Gels obtained from double-heated dispersions had lower values of shear strain and shear stress at fracture than gels obtained from single-heated dispersions. Double heating caused a significant complex modulus (G*) increase at 4% WPI and 15 mm calcium ions in comparison with gels obtained from single-heated dispersion. Less significant differences between gels made from double and single-heated dispersions were observed at 6% WPI, however a higher value of complex modulus was obtained for 8% protein gels from the single-heated solution. Native and non-reduced SDS–PAGE did not show clearly the effect of different procedures of heating on the quantities of polymerised proteins. Proteins in double-heated dispersions had higher hydrophobicity. Increased calcium concentration caused decreased protein hydrophobicity for both single and double-heated solutions.     

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.     

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 transglutaminase on rheological properties and microstructure of chemically acidified sodium caseinate gels

The mechanical properties and microstructure of 2.7% and 4.5% sodium caseinate gels chemically acidified by glucono-δ-lactone (GDL) and cross-linked by microbial transglutaminase (TG) were studied. The acidification was performed at different temperatures. According to SDS–PAGE TG clearly caused polymerisation of caseinate irrespective of the treatment temperature (4–50 °C), The cross-linking of the proteins was more extensive at temperatures 22–50 °C. Low amplitude viscoelastic measurements showed that 4.5% caseinate gels acidified at 50 °C were formed much faster than gels acidified at 22 °C. TG only slightly increased the time of gelling. Control gels prepared without TG at temperatures of 4, 22, 37 and 50 °C were mechanically weak. Examination of the control gels with a confocal laser scanning microscope showed that gels formed at 37 and 50 °C were coarse and porous with large cavities between particle aggregates, whereas those formed at 22 °C were much more homogeneous. The TG-treated and acidified sodium caseinate dispersions formed firm gels, indicating cross-linking of casein proteins. Interestingly, the strongest gels were formed at 22 and 37 °C. TG treatment improved the homogeneity of the gel structure at temperatures of 37 and 50 °C. The hardness of TG-treated gels acidified at 4 °C increased during 1 week of storage.     

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.     

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.     

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.