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.     

Stability of oil‐in‐water emulsions as influenced by thermal treatment of whey protein dispersions or emulsions

Properties of whey protein concentrate stabilised emulsions were modified by protein and emulsion heat treatment (60–90 °C). All liquid emulsions were flocculated and the particle sizes showed bimodal size distributions. The state and surface properties of proteins and coexisting protein/aggregates in the system strongly determined the stability of heat‐modified whey protein concentrate stabilised emulsions. The whey protein particles of 122–342 nm that formed on protein heating enhanced the stability of highly concentrated emulsions. These particles stabilised protein‐heated emulsions in the way that is typical for Pickering emulsions. The emulsions heated at 80 and 90 °C gelled due to the aggregation of the protein‐coated oil droplets.     

Analysis of the preferential mechanisms of denaturation of whey protein variants as a function of temperature and pH for the development of an optical sensor

A pH‐ and temperature‐dependent study was conducted using reconstituted low‐heat skim milk at pH 6.3, 6.7 and 7.1 heated for 10 min at 80 and 90 °C to evaluate the relationship between bound and aggregate whey protein and optical light backscatter response. Significant correlations were found between casein micelle particle size and bound whey protein, and light backscatter correlations existed with both bound and aggregate whey protein, thus optical light backscatter may be useful to determine both whey protein attachment to the casein micelle and the formation of whey protein aggregates.     

Calcium sulphate‐induced soya bean protein tofu‐type gels: influence of denaturation and particle size

Soya bean protein isolate (SPI) dispersions (7.25%, w/v) were heated at 65, 75, 85 or 90 °C for different time periods to produce SPI aggregates with diverse degrees of denaturation and particle size to investigate the effects on calcium sulphate (CaSO₄)‐induced tofu‐type gel. The results revealed that gel hardness and water‐holding capacity correlated positively with the degree of denaturation of glycinin (11S) and the particle size of the SPI aggregates. The formed gels showed more uniform and denser network structures with increasing degrees of denaturation and particle size of SPI. Hydrophobic interaction was speculated to be the crucial factor for the retention of gels prepared by SPI whose degree of denaturation by 11S was lower than 4.35%. However, disulphide bonds probably played a more important role in the retention of gels generated by SPI with the 11S denaturation degree of >84.47%. Moreover, the bulk density of the protein aggregates might determine the gel structures to a certain extent.     

High pressure versus heat treatments for pasteurisation and sterilisation of model emulsions

Heat treatments can have considerable influence on the droplet size distribution of oil-in-water emulsions. In the present study, high-pressure (HP) pasteurisation and sterilisation were evaluated as alternatives for heat preservation of emulsions. HP conditions used were 600 MPa, 5 min, room temperature and 800 MPa, 5 min, 80 °C initial temperature, 115 °C maximum temperature for HP pasteurisation and HP sterilisation respectively. The effects on droplet size of these conditions were compared to heat treatments for whey protein isolate (WPI) and soy protein isolate (SPI) emulsions at two pH values and two ionic strengths. For WPI, also the effect of protein in the bulk phase was evaluated.Both HP and heat pasteurisation treatments resulted in similar or slightly decreased average droplet sizes compared to the untreated samples. For neutral SPI emulsions, heat sterilisation increased the average droplet size from 1.6 μm to 43.7 μm, while HP sterilisation resulted only in a small increase towards an average droplet size of 2.1 μm. The neutral WPI emulsions, except those with a high ionic strength, gave similar results with respect to the droplet size, showing that for neutral pH WPI or SPI emulsions HP sterilisation is preferable above heat sterilisation. Concerning the low pH WPI emulsions, the droplet sizes were unaffected after both heat and HP sterilisation.Industrial relevanceHeat pasteurisation and sterilisation are effective treatments to preserve food products that are based on emulsions with respect to microbial safety. However, heat treatments can negatively affect emulsion stability. Currently, in addition to high pressure at room temperature, high-pressure treatments at elevated temperature received a great deal of interest to achieve sterilised products. This study evaluated the effects of both heat and high-pressure pasteurisation and sterilisation on droplet size of whey protein isolate and soy protein isolate emulsions. It was shown that for pasteurisation treatments, both heat and high pressure have minor effects on the droplet size of the emulsion. However, for sterilisation purposes high-pressure treatment is preferable for emulsion at neutral pH. High-pressure sterilisation can therefore be interesting alternatives to heat treatments to preserve emulsion stability.     

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.     

Effect of limited enzymatic hydrolysis on physico‐chemical properties of soybean protein isolate‐maltodextrin conjugates

The effect of limited hydrolysis was investigated on the physico‐chemical properties of soy protein isolate–maltodextrin (SPI‐Md) conjugate. The hydrolysates at a degree of hydrolysis (DH) of 1.8% showed much higher surface hydrophobicity (H₀; 71.39 ± 3.60) than that of the SPI control (42.09 ± 2.17) and SPI‐Md conjugates (53.46 ± 2.74). Intrinsic fluorescence analysis demonstrated the unfolding of protein molecule and exposure of hydrophobic groups of SPI‐Md conjugate hydrolysates. As evidenced by far‐UV circular dichroism (CD) spectroscopy, the limited hydrolysis increased the unordered secondary structures of SPI‐Md conjugates. The denaturation temperature (T_d) of SPI‐Md conjugate was significantly increased by subsequent limited hydrolysis from 102.53 ± 0.60 °C to 108.11 ± 0.61 °C at DH 1.8%. In particular, the emulsifying activity index (EAI) was improved notably after limited hydrolysis of DH 1.8% (147.76 ± 4.39 m² g^?1) compared with that of native SPI (88.90 ± 1.44 m² g^?1) and SPI‐Md conjugate (108.97 ± 1.45 m² g^?1).     

Effect of frozen storage on thermal stability of sarcoplasmic protein and myofibrillar protein from common carp (Cyprinus carpio) muscle

Thermal stability of sarcoplasmic protein and myofibrillar protein extracted from fresh and frozen common carp was comparatively studied. Total sulphydryl content (SH) in sarcoplasmic protein solution from 5‐month frozen carp decreased by 19.43% compared with fresh sample. The SDS‐PAGE patterns showed that all the bands of sarcoplasmic protein from frozen‐stored samples were almost invisible at 80 °C. Myofibrillar protein from fresh sample exhibited lower turbidity and surface hydrophobicity and higher Ca²⁺‐ATPase activity and SH content than frozen‐stored sample when heated from 20 to 80 °C. The Ca²⁺‐ATPase activity from fresh (M0), 2 (M2)‐ and 5 (M5)‐month frozen‐stored carp was completely lost at 48, 46 and 46 °C, respectively. When heated to 80 °C, the SH content of myofibrillar solutions in M0, M2 and M5 decreased by 26%, 60% and 70%, respectively. Sarcoplasmic and myofibrillar proteins from frozen carp were more susceptible to aggregate during heating treatment.     

Structure,composition and functional properties of storage proteins extracted from bambara groundnut (Vigna subterranea) landraces

Bambara groundnut is a protein‐rich traditional legume. In this study, storage proteins were isolated from three bambara landraces. Bambara protein revealed four major protein bands: one broad band at 55 kDa, two medium bands at 62 kDa and 80 kDa and a high molecular weight (HMW) protein at 141 kDa. The vicilin (7S) subunits with molecular weight of 55 kDa and 62 kDa were major fractions in bambara storage proteins. Bambara proteins showed two endothermic peaks ranging from 64 to 69 °C and 76 to 90 °C, respectively. Bambara protein isolates had well‐defined tertiary and secondary structures, respectively, at pH 3.0, and this well‐defined structure decreased slightly at higher pH values. The isolates revealed a strong secondary structure dominated by α‐helical conformation. Foaming capacities of bambara proteins were dependent on pH with maximum percentage FC observed at pH 3.0, while the emulsion activity increased with increasing pH for all the isolates. Vicilin (7S) fraction seems to be the major storage protein fraction of bambara. Bambara proteins could serve as excellent ingredients for the formulation of food foams and emulsions.     

Chitosan/tripolyphosphate‐nanoliposomes core‐shell nanocomplexes as vitamin E carriers: shelf‐life and thermal properties

The aim of this study was to prepare the new core‐shell nanocomplexes as vitamin E (VE) carriers through chitosan (CS) coating onto the liposomal membrane surface in combination with sodium tripolyphosphate (TPP) cross‐linking, and investigated their storage and thermal properties by dynamic light scattering, ζ potential and fluorescence. Results showed that no obvious aggregation of nanocomplexes particles appeared and the VE retention rate was over 80% during the 30‐day storage. Thermal experiments demonstrated that the modification of polymers enhanced the stability of liposomes against temperature, including suppressing particle aggregation, ζ potential inversion and membrane fluidity. Compared with the great leakage of VE from uncovered liposomes, the retention rate of VE loaded into nanocomplexes remained around 92% and 97% after heated at 65 °C for 30 min and 80 °C for 16 s, respectively. The findings proved that these nanocomplexes can be employed to protect VE for extending shelf‐life and enhancing thermostability, and provide feasibility for commercial usage.     

Stability and mechanism of whey protein soluble aggregates thermally treated with salts

The formation of whey protein aggregates, often termed soluble aggregates, with specific physicochemical properties has been shown to result in improved functionality in gels, foams, emulsions, encapsulation, films and coatings. This work evaluated the potential of whey protein soluble aggregates to improve thermal stability in the presence of salts and determine the mechanism of improved thermal stability. Solutions of whey protein isolate (WPI) or β-lactoglobulin (β-lg) (7% w/w, pH 6.8) were heated for 10 min at 90 °C to form soluble aggregates. Native proteins and soluble aggregates were diluted to 3% w/w in solutions containing 0–108 mM NaCl and thermally treated (90 °C, 5 min). Turbidity, solubility, and viscosity were evaluated, in addition to ζ-potential and S_o (surface hydrophobicity). Size exclusion chromatography coupled with multi-angle laser light scattering (SEC-MALLS) and dynamic light scattering were used to determine aggregate size and transmission electron microscopy (TEM) was used to evaluate aggregate shape. Use of soluble aggregates improved thermal stability due to their altered aggregate shape and higher charge, and resulted in final aggregates that were smaller and less dense, leading to reduced viscosity and turbidity, and increased solubility compared to native proteins. It is concluded that soluble aggregates formed under the appropriate conditions to produce the desirable physicochemical properties can be used to improve whey protein thermal stability with a possible application in beverages.     

Formation and stability of emulsions stabilised by Yucca saponin extract

Yucca saponin extract containing steroidal saponins was examined for its interfacial and emulsifying properties. For this purpose, we produced oil‐in‐water emulsions and tested their stability against environmental stresses (pH, ionic strength, heating and freeze‐thawing). Yucca saponin extract was highly surface‐active and formed negatively charged submicron‐sized emulsions at low surfactant‐to‐oil ratio. The emulsions were stable at pH 5–9 and showed only minor increase in droplet size when heated up to 90 °C. Our results indicate Yucca saponin extract as a new potential natural surfactant that may be used to replace synthetic surfactants in the food and beverage industry for selected applications.     

Preparation,characterisation and selected functional properties of hydrolysed sodium caseinate–maltodextrin conjugate

Sodium caseinate was hydrolysed to a limited, moderate or extensive degree. The hydrolysates were conjugated with maltodextrin by a Maillard‐type reaction by dry‐heat treatment at 60 °C and 79% relative humidity for 2 or 4 days. Conjugates were characterised by SDS–PAGE and gel permeation chromatography. In comparison with the hydrolysates themselves, the conjugated hydrolysates had improved solubility, particularly around the isoelectric pH of the protein. The emulsifying properties of these conjugates were assessed in oil‐in‐water (o/w) emulsions; on emulsion formation, each conjugate‐stabilised emulsion had lower mean fat globule size than the corresponding hydrolysate‐stabilised emulsion. After storage for 7 days under accelerated shelf life testing conditions, the limited and moderate hydrolysate conjugate–stabilised emulsions had improved storage stability compared with hydrolysate‐stabilised emulsions; however, further research is required to optimise the hydrolysate fraction prior to conjugation for the production of novel low molecular weight emulsifiers.     

Characterisation of soluble aggregates from commercial whey protein concentrate suspensions: Effect of protein concentration,pH, and heat treatment conditions

Soluble aggregates obtained from heat‐treated suspensions of commercial whey protein concentrate with 74.4% w/w protein were characterised. The effect of protein concentration (7 and 8% w/w), pH (7.0, 7.5 and 8.0), and heating time (0, 5, 10, 15, 20 and 30 min) at 80 °C were evaluated. Whey protein concentrate suspensions with the highest protein concentration (8% w/w) and the lowest pH (pH 7.0) had the highest steady shear viscosity and absorbance values, indicating the effect of the soluble aggregate content (high concentration) and the aggregate size (at lower pH values). According to principal component analysis, samples with 8% w/w and pH 7.0 were grouped in a plot region that confirmed the behaviour observed by confocal microscopy. Those whey protein concentrate suspensions could have soluble aggregates with a strong probability of interacting with cations (in cold gelation applications such as microencapsulation) and with each other (in film‐formation during coating).     

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.     

高温短时干热法制备SPI-麦芽糊精糖基化产物及其乳化性的研究

采用高温(90,115和140℃)短时(2 h)干热法制备了大豆分离蛋白(SPI)-麦芽糊精(MD)糖基化产物。利用接枝度和SDS-PAGE研究了SPI与MD发生糖基化反应的程度。同时考察了SPI-MD糖基化产物稳定水包油乳液的性质,并探讨了盐离子和热处理对SPI-MD糖基化产物稳定乳液的储藏稳定性的影响。试验发现,提高反应温度能增大糖基化反应的接枝度,且pH 3.0时,与添加盐离子或经过热处理的SPI,SPI-MD糖基化产物(90℃)和SPI-MD糖基化产物(115℃)稳定乳液相比,添加盐离子或经过热处理的SPI-MD糖基化产物(140℃)的稳定的乳液具有较高的乳化稳定性和储藏稳定性。     

The influence of enzymatic cross‐linking of proteins on the Maillard reaction in milk

The influence of transglutaminase (TGase) on the Maillard reaction was investigated in skimmed milk samples during heat treatment. TGase‐treated and control samples were heated at 80, 120 and 140 °C for 1, 5, 15, 30, 40 and 60 min. Compared with the TGase‐treated samples heated at 80 and 120 °C, the sample heated at 140 °C showed a larger decrease in furosine concentration. It was also found that TGase did not affect the formation of hydroxymethylfurfural and lactulose at 120 °C, whereas their concentrations increased in the presence of TGase at 140 °C. It was concluded that blockage of lysine residues via enzymatic cross‐linking of milk proteins had a limited effect on the Maillard reaction.     

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.     

Particle size determines foam stability of casein micelle dispersions

The role of interfacial properties and size of casein micelles aggregates on foam stability of casein micelle dispersions (CMDs) was examined. CMDs were prepared by redispersing casein micelles pellets obtained by ultracentrifugation. The size of colloidal particles could be controlled by differences in redispersing temperature. CMDs redispersed at 20 °C (CMD_20 °C) and 4 °C (CMD_4 °C) had average particle sizes of around 200 nm (micelles) and 500 nm (micelles and aggregates), respectively. At 3% total protein, the foam half-life, t_½, of CMD_4 °C was significantly higher than that of CMD_20 °C and skim milk. No correlation between foam stability and surface rheological properties or protein composition could be observed. Foam stability was strongly related to the size of colloidal particles present in CMD. This was confirmed by the observation that the foam stability of CMD_4 °C decreased to that of CMD_20 °C when the aggregates were broken down by homogenisation.     

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.