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.     

Interactions and gel strength of mixed myofibrillar with soy protein, 7S globulin and enzyme-hydrolyzed soy proteins

The mixed protein gels were prepared adding soy protein isolate (SPI), 7S globulin, enzyme-hydrolyzed soy proteins, 10- to 100-kDa ultrafiltration fraction and 0.5- to 10-kDa ultrafiltration fraction to myofibril protein isolate (MPI) gels, and five chemical interactions namely nonspecific associations, ionic bonds, hydrogen bonds, hydrophobic interactions and disulfide bonds in these gels were investigated by means of determining gel solubility within 20–75 °C. Furthermore, correlations between gel strength and different chemical interactions were evaluated statistically by Pearson’s correlation test. The gels with 0.5- to 10-kDa fraction presented the biggest gel strength below 60 °C, and the gels with SPI had better gel strength above 65 °C. At different endpoint temperatures, nonspecific associations decreased in order of MPI mixed with 0.5- to 10-kDa fraction, 10- to 100-kDa fraction, enzyme-hydrolyzed soy proteins, 7S globulin and SPI. Gels with ultrafiltration fractions had higher ionic bonds. Hydrogen bonds fluctuated in small scale below 55 °C and reduced at higher temperature. Hydrophobic interactions increased to maximum before decreasing slowly as the temperature went on. In short, both hydrophobic interactions and ionic bonds had significantly positive correlation with gel strength for mixed gels with enzyme-hydrolyzed soy proteins, whereas for the other four mixed gels, it was hydrophobic interactions and nonspecific associations.     

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.     

Physical properties of emulsion gels formulated with sonicated soy protein isolate

This study aimed to determine the effect of high-intensity ultrasound (HIU) on physical properties of soy protein isolate dispersions (SPI) and their addition to emulsion gels (EG) containing soybean oil (SBO), inulin (IN) and carrageenan (CAR). Sonicated and non-sonicated SPI dispersions were mixed with CAR, IN and SBO and heated at 90 °C for 30 min to gel the emulsion. An increase in solubility and oil binding capacity was observed in sonicated SPI dispersions (S-SPI) compared to the non-sonicated ones. HIU changed the molecular weight of SPI and decreased apparent viscosity in the dispersions. The use of S-SPI in the EG reduced the droplet size and increased the hardness and G′ values. The use of S-SPI allowed a reduction of 75% of carrageenan in the EG without affecting the hardness of the gel. The results suggest that HIU can be used to improve rheological properties of functional EG.     

Gelation enhancement of soy protein isolate by sequential low‐ and ultrahigh‐temperature two‐stage preheating treatments

The effects of combined two heating steps with low (LT, 60 °C for 1 h) and ultrahigh (UHT, 130 or 140 °C for 4 s) temperatures on the thermal gelation of soy protein isolate (SPI) were studied. UHT pretreatments significantly increased protein solubility and enhanced the gelling potential of SPI. Yet, the two‐stage preheating treatment with LT and then UHT‐130 °C had a most remarkable effect: the gel strength of the SPI₆₀₊₁₃₀ sample was, respectively, 1.45‐, 1.64‐ and 3.19‐fold as strong as those of SPI₆₀, SPI₂₅₊₁₃₀, and SPI₂₅. In comparison with single LT or UHT treatments, this two‐stage heating also produced greater amounts of soluble protein aggregates stabilised predominantly by disulphide bonds and hydrophobic forces, contributing to the improved gel network structure.     

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.     

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.     

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.     

Comparative studies on the physicochemical properties of soy protein isolate-maltodextrin and soy protein isolate-gum acacia conjugate prepared through Maillard reaction

Dry-heated Maillard reaction was applied in the preparation of protein–polysaccharide conjugates. Reaction mixtures containing soy protein isolate (SPI) and maltodextrin (1:1 weight ratio) were dry-heated at 60 °C and 79% relative humidity for three days. The mixtures of SPI and gum acacia (GA) were dry-heated at the same condition for one week. The conjugate of SPI–MD showed lower levels of free amino groups and higher degree of graft, which indicated that reaction between SPI and MD developed much faster than reaction between SPI and GA. The solubility of SPI at isoelectric point was improved remarkably after grafting with MD or GA. The grafted SPI showed significantly higher levels of emulsifying properties than SPI and the emulsifying properties of SPI–GA conjugate were much better than SPI–MD. Decreases of lysine and arginine contents after the graft reaction indicated that these two amino acid residues attended the covalent linkage between SPI and MD or GA. The graft reaction reduced surface hydrophobicity and fluorescence emission maximum value because of a shielding effect of the polysaccharide chain bound to proteins. The results of secondary structure suggested that grafted SPI had decreased the levels of α-helix, β-sheet and β-turn and increased unordered coils level.     

Effect of pulsed electric field on the secondary structure and thermal properties of soy protein isolate

Changes of structure and thermal stability of soy protein isolate after pulsed electric field treatment were analyzed by Fourier transform infrared spectroscopy and differential scanning calorimetry (DSC). When the applied pulsed electric field (PEF) treatment intensity was over 35 kV/cm, the amino acid side chain, anti-parallel β-sheets, β-turn as well as β-sheets in soy protein isolate (SPI) secondary structure were significantly changed, which suggested that PEF treatment might be a new processing method for SPI; the dipole moments of some bonds, such as C=O, C–O, and C–O–C were partially polarized, accompanying with complete denaturation of β-conglycinin and glycinin obtained from DSC. Furthermore, self-reassembly from β-turn to α-helix in SPI structure abruptly happened under intense PEF treatment condition, which suggested that the PEF treatment had induced change of the orientation of α-helix dipole moment to stabilize α-helix. This observation implies that PEF treatment technique may be a novel method for preparation of protein nanotube.     

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.     

Improvement in emulsifying properties of soy protein isolate by conjugation with maltodextrin using high‐temperature,short‐time dry‐heating Maillard reaction

Soy protein isolate (SPI)–maltodextrin (MD) conjugates were synthesised using Maillard reaction under high‐temperature (90, 115 and 140 °C), short‐time (2 h) dry‐heating conditions. The loss of free amino groups in proteins and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS‐PAGE) profile confirmed that SPI‐MD conjugates were formed and higher dry‐heated temperatures could increase the glycosylation degree. The emulsifying properties of SPI and SPI‐MD conjugates were evaluated in oil‐in‐water emulsions. The emulsions stabilised with SPI‐MD conjugates synthesised at 140 °C exhibited higher emulsifying stability and excellent storage stability against pH, ionic strength and thermal treatment compared with those synthesised at 90 °C, 115 °C and SPI stabilised emulsions. This might be due to a greater proportion of conjugated MD in SPI‐MD conjugates synthesised at 140 °C because of the higher glycosylation degree, and more conjugated MD on the droplet surface could provide steric effect and enhance the stability of the droplets in the emulsions.     

Amylose Chain Association Based On Differential Scanning Calorimetry

Amylose and lipid depleted starches from amylomaize, pea, maize, wheat, potato, and waxy maize were heated from 20°C to 180°C, cooled to 4°C, and then reheated to 180°C in a differential scanning calorimeter (DSC) in excess water. Cooling curves of the amylose and starch melts showed exothermic transitions (< 70°C) attributed to the mechanism of amylose chain association. Amylose/amylopectin mixtures covering the range 0–95% amylose were similarly heated and cooled. The association of linear amylose chains was restricted by amylopectin.     

Influence of enzyme active and inactive soy flours on cassava and corn starch properties

The aim of this work was to study the influence of enzyme active and inactive soy flours on the properties of cassava and corn starches. Four starch/soy flour composites were evaluated: cassava/active soy flour (Cas/AS), cassava/inactive soy flour (Cas/IS), corn/active soy flour (Corn/AS) and corn/inactive soy flour (Corn/IS). Starch gelatinization occurred at 58.67°C for Cas and at 64.19°C for corn; gelatinization occurred at higher temperatures when soy flours were present, while ΔH diminished. The presence of AS reduced 80% the retrogradation enthalpy of Cas and 40% that of corn. Cas presented lower pasting temperature than corn starch (67.8 and 76.8°C, respectively) and higher peak viscosity (427.9 and 232.8 BU, respectively). The pasting properties of both starches were drastically reduced by soy flours, and this effect was more noticeable in Cas; AS had higher effect than IS. X‐ray diffraction pattern of retrograded samples showed that both starches recrystallisation (mainly that of Cas) was reduced when AS was added. Tan δ values decreased with AS addition to corn, but they increased when added to Cas. The images obtained using confocal laser scanning microscopy (CLSM) showed that IS was distributed as large aggregates, whereas AS distribution was more homogeneous, especially when incorporated to Cas. These results show that cassava starch interacts specifically with active soy flour (AS, mainly in native state). The delaying effect of AS on cassava starch retrogradation was clearly shown. This finding could be useful in obtaining gluten‐free breads of high quality and low retrogradation rate.     

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.     

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.     

Effect of soy protein isolate on gel properties of Alaska pollock and common carp surimi at different setting conditions

The effects of soy protein isolate (SPI) on the gel properties of different grade Alaska pollock and common carp surimi at different setting conditions were evaluated and compared. Breaking force and distance of gels decreased with increasing SPI concentrations in direct cook (85 °C for 30 min) and in cook after setting at 30 °C for 60 min conditions. The effect of SPI on gel strength of common carp surimi was less than in Alaska pollock surimi. The breaking force obtained for addition of 10% SPI to Alaska pollock surimi was higher than for surimi alone when cooked after incubation at 50 °C for 60 min. Addition of SPI decreased the whiteness and increased the yellowness of the gel. The gel structure showed that the addition of SPI modified the microstructure of the fish protein gel, thus resulting in surimi with different gelling properties. Copyright © 2004 Society of Chemical Industry     

Textural properties and morphology of soy 7S globulin-corn starch (amylose,amylopectin)

The texture properties (hardness, adhesiveness, cohesion, elasticity) of composite gels with different ratios (0:100, 6:94, 8:92, 10:90, 12:88, and 14:86, respectively) of soy 7S globulin to corn starch (amylose, amylopectin) were studied. Furthermore, the morphology and crystal structure of the mixed gels were investigated. The results showed: the addition of soy 7S globulin could weaken the hardness of corn starch (amylose, amylopectin) and increased the adhesiveness of corn amylose significantly (p < 0.05). Generally, when the additive amount of soy 7S globulin was 10%, the composite gels of soy 7S globulin and corn starch (amylose, amylopectin) appeared to have the best consistency, cohesion, and elasticity.     

Morphological,Thermal, Pasting,and Rheological Properties of Barley Starch and Their Blends

Native barley starch, as well as its blends with corn, wheat, and rice starch at different ratios of 75:25, 50:50, 25:75 were examined in terms of morphology, thermal, pasting, rheological, and retrogradation properties. Amylose content varied between 10.9–41.4% in rice, corn, wheat, and barley while it ranged from 18.02–38.40% in blends of barley starch with rice, corn, and wheat. A rapid visco analyzer showed that barley starch and its blends having low amylose content exhibited higher peak viscosity, breakdown, and setback than the high-amylose-containing starches and their blends. Amylose content was found to be negatively correlated with swelling power while it exhibited nonlinear relationship with solubility index. The transmittance of starch suspension stored at 4°C decreased during storage up to 6 days. Barley starch granules were largest (<110 μm) in size followed by wheat (<30 μm), corn (<25μm) and rice (<20μm) starches. Gelatinization temperatures (To, Tp, Tc) and enthalpies of gelatinization (ΔHgel) of starches from different sources also differed significantly. Corn and rice starches showed higher transition temperatures in general than those from wheat and barley; however, they showed higher ΔHgel values. Barley starch showed a higher tendency towards retrogradation than the cereal starches. Barley starch showed highest peak G′, G″ and lower tan Ð than corn, rice and wheat starches during the heating cycle. This study showed that the magnitude of changes in their properties during blending depends on the amylase content and morphological characteristics.