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.     

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).     

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.     

Gel‐forming ability of surimi from grass carp (Ctenopharyngodon idellus): influence of heat treatment and soy protein isolate

The effects of setting conditions and soy protein isolate (SPI) on textural properties of surimi produced from grass carp were investigated. Effects of setting temperature, setting time and protein concentration on the breaking force and distance were evaluated and compared utilizing response surface methodology. Models for breaking force and breaking distance of grass carp surimi were established. Protein concentration was the major factor affecting the gel strength of grass carp surimi. Breaking force and distance of grass carp surimi gels decreased with increase of protein ratio from SPI at 30 °C and 40 °C for 60 min setting and heating at 85 °C for 30 min, but the breaking force obtained for addition of 100 g kg^?1 SPI protein to grass carp surimi was higher than that for surimi alone at 60 °C for 60 min incubation and heating at 85 °C for 30 min. Copyright © 2005 Society of Chemical Industry     

Zinc‐loaded whey protein nanoparticles prepared by enzymatic cross‐linking and desolvation

Zinc‐loaded whey protein nanoparticles were prepared by enzymatic cross‐linking whey protein followed by ethanol desolvation. Whey protein isolate (WPI) was denatured by heating (80 °C for 15 min) at pH 7.0 and then cross‐linked by transglutaminase at 50 °C for 4 h while stirring. Transglutaminase was inactivated by heating at 90 °C for 10 min, and then, ZnSO₄·7H₂O (1–10 mm ) was added. Zinc‐loaded whey protein nanoparticles were formed by adding ethanol at one to five times the volume of the protein solution at pH 9.0. The desolvated solutions were diluted by adding distilled water at ratio of 1:100 (w/v) immediately after desolvation. Dynamic light scattering (DLS) data showed that the particle size of zinc‐loaded whey protein nanoparticles increased with the amount of zinc and the volume of ethanol. Scanning electron microscopy micrographs revealed an almost spherical morphology for zinc‐loaded whey protein nanoparticles. The zinc loading efficiency was determined ranging from 76.7% to 99.2%. In vitro test data showed that the zinc release rate was low in simulated gastric fluid but high in simulated intestinal fluid. The results indicated that enzymatic cross‐linked whey protein nanoparticles may be used as a good vehicle to deliver zinc as a supplement.     

Surface Properties of Heat‐Induced Soluble Soy Protein Aggregates of Different Molecular Masses

Suspensions (2% and 5%, w/v) of soy protein isolate (SPI) were heated at 80, 90, or 100 °C for different time periods to produce soluble aggregates of different molecular sizes to investigate the relationship between particle size and surface properties (emulsions and foams). Soluble aggregates generated in these model systems were characterized by gel permeation chromatography and sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. Heat treatment increased surface hydrophobicity, induced SPI aggregation via hydrophobic interaction and disulfide bonds, and formed soluble aggregates of different sizes. Heating of 5% SPI always promoted large‐size aggregate (LA; >1000 kDa) formation irrespective of temperature, whereas the aggregate size distribution in 2% SPI was temperature dependent: the LA fraction progressively rose with temperature (80→90→100 °C), corresponding to the attenuation of medium‐size aggregates (MA; 670 to 1000 kDa) initially abundant at 80 °C. Heated SPI with abundant LA (>50%) promoted foam stability. LA also exhibited excellent emulsifying activity and stabilized emulsions by promoting the formation of small oil droplets covered with a thick interfacial protein layer. However, despite a similar influence on emulsion stability, MA enhanced foaming capacity but were less capable of stabilizing emulsions than LA. The functionality variation between heated SPI samples is clearly related to the distribution of aggregates that differ in molecular size and surface activity. The findings may encourage further research to develop functional SPI aggregates for various commercial applications.     

Low‐field nuclear magnetic resonance analysis of the effects of heating temperature and time on braised beef

We investigated the characteristics of water mobility and distribution in Chinese braised beef after treatment at different temperatures for different times using low‐field nuclear magnetic resonance (LF‐NMR). The beef was heated at 45, 55, 65, 75, 85 or 95 °C for 30, 60, 90 and 120 min. Results showed that T₂ changed significantly with heating temperature. T₂₁ and A₂₁ decreased significantly with increasing temperature below 65 °C, with a steady phase from 75 to 95 °C, which agreed with cooking loss. Inversely, T₂₂ had no changes below 65 °C and changed apparently from 75 to 95 °C. The change in T₂₁ below 65 °C may be related to proteins denaturation and shrinkage and, above 65 °C, T₂₂ possibly induced by the dissolution of connective tissue. The characteristics of braised beef at 65 °C were different from those at other temperatures in T₂ distributions. The findings could provide a theoretical basis for the processing of Chinese braised beef.     

Drying characteristics and thermal degradation kinetics of hardness,anthocyanin content and colour in purple‐ and red‐fleshed potato (Solanum tuberosum L.) during hot air drying

Purple‐fleshed potatoes (PFP) and red‐fleshed potatoes (RFP) were dried using hot air. The hardness, anthocyanin content and colour in PFP and RFP during drying were evaluated at 60, 70 and 80 °C. The hardness was characterised by a softening stage in the early drying period, followed by a hardening stage. The times to reach at the transition were 420, 300 and 240 min at 60, 70 and 80 °C, respectively, for PFP, and 480, 360 and 240 min for RFP. However, the moisture content of both PFP and RFP at the transition time was identical at 0.3 (d.b.). The two stages of hardness changes were well described by combining two modified first‐order kinetics models. The activation energy (E_a) for the degradation of anthocyanin in PFP and RFP was 25.12 and 28.43 kJ mol^?1, respectively. The E_a values demonstrated that the thermal sensitivity of PFP was higher than that of RFP.     

Rennet coagulation properties of UHT‐treated phosphocasein dispersions as a function of casein and NaCl concentrations

The renneting properties of whey protein‐free, UHT‐heated (140 °C/10 s) casein dispersions were investigated as a function of casein and NaCl concentration. It was found that the rennet coagulation time and gel firmness can be optimised when the whey protein‐free casein concentration is increased, while the added NaCl concentration is kept low. The strongest gel firmness occurs at 0.05 and 0.08 m NaCl addition and at a micellar casein concentration between 6.0 and 6.6 g/100 mL. Weak rennet gels were formed at 3.0–3.6 g/100 mL casein at all NaCl concentrations tested.     

Interaction of Protein Isolate with Anthocyanin Extracted from Black Soybean and Its Effect on the Anthocyanin Stability

The interactions between black soybean protein isolate (B‐SPI) and cyanidin 3‐O‐glucoside (C3G), anthocyanin extracted from black soybean coat was investigated under neutral conditions. The fluorescence spectra showed that C3G had fluorescence quenching effects on B‐SPI. Thermodynamic parameters showed that ? G < 0, which demonstrated that the binding was a spontaneous reaction. Since ΔH > 0 and ΔS > 0, the interactions between C3G and B‐SPI was mainly hydrophobic interactions. Fourier infrared spectroscopy results suggested that the contents of α‐helix and β‐sheet structure showed an increasing trend, whereas the β‐angle content displayed a decreasing trend. The degradation of C3G followed first‐order kinetics at 85 °C and 100 °C. After the interactions with B‐SPI, the degradation rate constant was decreased and the half‐life of C3G was prolonged from 70.25 ± 0.90 min to 175.64 ± 38.04 min at 85 °C, from 62.68 ± 1.1 min to 72.51 ± 2.5 min at 100 °C (p < 0.05). The results indicated that the interactions of B‐SPI and C3G improved the thermal stability of C3G under heating conditions.     

Interaction of β‐casein with (−)‐epigallocatechin‐3‐gallate assayed by fluorescence quenching: effect of thermal processing temperature

The interactions between the flavan‐3‐ol (?)‐epigallocatechin‐3‐gallate (EGCG) and bovine β‐casein in phosphate‐buffered saline (PBS) of pH 6.5 subjected to thermal processing at various temperatures (25–100 °C) were investigated using fluorescence quenching. The results indicated that different temperatures had different effects on the structural changes and EGCG‐binding ability of β‐casein. At temperatures below 60 °C, the β‐casein–EGCG interaction changed little (P > 0.05) with increasing temperature. At temperatures above 80 °C, native assemblies of β‐casein in solution dissociated into individual β‐casein molecules and unfolded, as demonstrated by a red shift of the maximum fluorescence emission wavelength (λ_max) of up to 8.8 nm. The highest quenching constant (K_q) and the number of binding sites (n) were 0.92 (±0.01) × 10¹³ m ^?1 s^?1 and 0.73 (±0.02) (100 °C), respectively. These results provide insight into the potential of interactions between β‐casein–EGCG that may modulate bioactivity or bioavailability to be altered during thermal process.     

Enhancing the antioxidant activity of immature calamondin by heat treatment

The purpose of this study was to investigate the enhancing effect of heat treatment (110 and 130 °C for 0.5, 1.0, 1.5 and 2.0 h, and 150 °C for 1.5 h) on antioxidant activity and phenolic compounds of immature calamondin (Citrus mitis Blanco). The results indicated that heat treatment could enhance the 2,2‐diphenyl‐1‐picrylhydrazyl (DPPH) scavenging potency, oxygen radical absorbance capacity (ORAC) and total phenolic content. However, the major flavonoid, 3′,5′‐di‐C‐β‐glucopyranosylphloretin (DGPP), decreased drastically after being heated at ≥130 °C over 1.5 h. The increasing ratio of absorbance at UV₄₂₀ nm coincided with the change of the antioxidant activity. Therefore, it was concluded that the browning products resulted in the increase of the antioxidant activity of immature calamondin heated at ≥130 °C over 1.5 h, while the increase of antioxidant activity at 110 and 130 °C ≤ 1.0 h heating was due to increased phenolic content.     

Effects of microwave and hot‐air drying methods on colour, β‐carotene and radical scavenging activity of apricots

The effects of drying by microwave and convective heating at 60 and 70 °C on colour change, degradation of β‐carotene and the 2,2‐diphenyl‐1‐picrylhydrazyl radical (DPPH) scavenging activity of apricots were evaluated. Microwave heating reduced significantly the drying time (up to 25%), if compared with convective one, also owing to the higher temperature reached during the last phase of the process, as monitored by infrared thermography. Colour changes of apricot surface, described with lightness and hue angle, in both drying methods followed a first‐order reaction (0.927 ≤ R² ≤ 0.996). The apricots dried by microwave were less affected by the darkening phenomena. The evolution of β‐carotene in fresh apricots (61.2 ± 5.6 mg kg^?1 d.w.) during the drying highlighted a wider decrease (about 50%) when microwave heating was employed for both the temperatures used. Radical scavenging activity increased (P < 0.05) in all dried samples except for hot‐air dried apricots at 60 °C.     

The effect of pH and calcium ion on rheological behaviour of β‐lactoglobulin‐basil seed gum mixed gels

Effect of pH (4.5–7.5) and Ca²⁺ (0.01–0.5 m ) on gelation of single and mixed systems of 10% β‐lactoglobulin (BLG) and 1% basil seed gum (BSG) was investigated. The gelling point of BLG and BSG gels was strongly pH‐dependent, and stiffer gels formed at higher pH. The BLG gels were formed upon heating to 90 °C and reinforced on cooling to 20 °C; however, the gelation of BSG occurred at temperatures below 70 °C. By increasing Ca²⁺ concentration, storage modulus of BLG and BSG gels were increased, although pH had a greater effect than Ca²⁺. In contrast, mixed systems showed two distinct types of behaviour: BLG gel formation and BSG network, suggesting that phase‐separated gels were formed. In addition, higher strength was obtained for BLG‐BSG mixture at higher Ca²⁺ concentration.     

Formation of acid‐precipitated soy protein–dextran conjugates by Maillard reaction in liquid systems

The conjugation reaction between soybean acid‐precipitated protein (SAPP) and dextran in liquid systems via the initial stage of the Maillard reaction was studied. Functional SAPP–dextran conjugates were prepared in 80% ethanol‐reacting system at 50 °C for 6 h, along with 95% ethanol‐reacting system at 60 °C for 24 h. The covalent attachment of dextran to SAPP was confirmed by sodium dodecyl sulphate–polyacrylamide gel electrophoresis and gel filtration chromatography.Compared to the classical dry‐heating, the reaction time of glycosylation in the two ethanol systems was largely shortened. Emulsifying activity of SAPP–dextran conjugates obtained by dry‐heating incubation and in ethanol was similar at pH 7.0 and10.0, significantly higher than that of SAPP–dextran mixture or SAPP alone. In addition, SAPP–dextran conjugates obtained in 80% ethanol‐reacting system for 6 h were completely soluble after heating at 90 °C for 20 min. The impact of various processing conditions on the formation of SAPP–dextran conjugates was investigated. This study provides important guidance to create protein–polysaccharide conjugates at mild temperatures in liquid systems.     

Microbiological safety of UHT milk treated at 120 °C for 2 s,as estimated from the distribution of high-heat-resistant Bacillus cereus in dairy environments

Unlike common ultra-high-temperature (UHT) milk, so-called “UHT milk” in Japan is typically pasteurised at 120–130 °C for 2 s and distributed at 10 °C or less, and there is a potential risk of Bacillus cereus. To estimate the microbiological safety of UHT milk, we surveyed the distribution of high-heat-resistant B. cereus strains (defined as showing <∼3 log reduction after treatment at 120 °C for 2 s) among 200 isolates from dairy environments. Only four strains, which were isolated from the milk plant environment, showed high-heat resistance. All of them were unable to grow at 10 °C but grew at 12 °C. In contrast, heat-labile strains grew well at 10 °C. Therefore, UHT milk pasteurised at 120 °C for 2 s can be microbiologically safe, provided it is kept at 10 °C or less, within a rational shelf-life and avoiding contamination with B. cereus, especially of milk-plant-environment origin.     

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.     

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.     

High‐pressure processing‐induced conformational changes during heating affect water holding capacity of myosin gel

This study aimed to investigate the effects of high‐pressure processing (HPP) (0.1‐400 MPa for 9 min) on the water holding capacity (WHC) of heat‐induced rabbit myosin gel and structural changes during thermal treatment (25–75 °C). HPP at 100 MPa significantly increased the WHC (P < 0.05) and formed more regular and homogeneous three‐dimensional network. Myosin tails at 100 MPa unfolded completely during the thermal treatment, which was beneficial to form a high WHC gel network. However, myosin pressurised at 200 MPa and above formed a weak gel. Their heads were already aggregated before heating, preventing from subsequent thermal denaturation and aggregation. With the temperature increasing, unfolding of myosin tails was not sufficient for a filamentous network formation. These results suggested that HPP could modify the myosin structure and affect the gel formation during heating. The 100 MPa was the optimum pressure level for the WHC of rabbit myosin gel.     

Nutritional properties of oat‐based beverages as affected by processing and storage

Oat‐based beverages enriched with vitamins and minerals were produced with common hydrothermal treatments and stored at 22 °C for 64 weeks. The effects of decanting on the retention of native vitamins, minerals and fatty acids, and different UHT holding time (5 s or 20 s) at 140 °C on vitamins were investigated. Fatty acid profile, vitamin retention and dissolved oxygen concentration were monitored during storage. The decanting process caused a 47% increase of vitamin B₆ and a 45–74% loss of phosphorus, zinc, calcium and iron. The steam‐injection UHT treatment caused a 60% loss of vitamin D₃ for both holding times and a 30% loss of vitamin B₁₂ for 20 s. During 1 year of storage, oleic and linoleic acids were stable, whereas linolenic acid decreased only slightly, even in the iron‐enriched variety. The dissolved oxygen concentration increased to a low value of 0.71 mg L^?1 and reached a balance after 16 weeks. Most enriched vitamins except vitamins A, D₃ and B₁₂ were stable during ambient storage. Oat‐based beverages with highly retained vitamins can be manufactured by adding vitamins prior to direct UHT treatment with a shorter holding time. Additionally, iron enrichment of such beverages, without affecting the fatty acid profile, can be achieved by filter sterilisation. Copyright © 2007 Society of Chemical Industry