Effect of high-intensity ultrasonic treatment on the emulsion of hemp seed oil stabilized with hemp seed protein

In this study, hemp seed oil (HSO) emulsions stabilized with hemp seed protein (HPI) were prepared and treated with high intensity ultrasonic (HIU). The effects of different treatment powers (0, 150, 300, 450, 600 W) on the properties, microstructure and stability of emulsions were investigated. HIU-treated emulsions showed improved emulsifying activity index and emulsifying stability index, reduced particle size, and increased absolute values of ζ-potential, with the extreme points of these indices occurring at a treatment power of 450 W. Here, the emulsion showed the best dispersion and the smallest particle size in fluorescence microscopy observation, with the highest adsorbed protein content (30.12%), and the highest tetrahydrocannabinol (THC) retention rate (87.64%). The best thermal and oxidative stability of the emulsions were obtained under HIU treatment with a power of 450 W. The D₄₃ and the peroxide values (POV) values after 30 d storage were the smallest at 985.74 ± 64.89 nm and 4.6 μmol/L, respectively. Therefore, 450 W was optimal HIU power to effectively improve the properties of HPI-stabilized HSO emulsion and promote the application of HSO and its derivatives in food processing production.     

Fabrication of emulsions prepared by rice bran protein hydrolysate and ferulic acid covalent conjugate: Focus on ultrasonic emulsification

The aim of the paper was to investigate the effect of ultrasonic emulsification treatment on the fabrication mechanism and stability of the emulsion. The covalent conjugate made with rice bran protein hydrolysate (RBPH) and ferulic acid (FA) was used as the emulsifier. The effects of high intensity ultrasound (HIU) power with different level (0 W, 150 W, 300 W, 450 W and 600 W) on the stability of emulsion were evaluated. The results showed that ultrasonic emulsification can significantly improve the stability of the emulsions (p < 0.05). The emulsion gained better stability and emulsifying property at 300 W. It was able to fabricate emulsion with smaller particle size, more uniform distribution and higher interfacial protein content. It was confirmed by fluorescent microscopy and cryo-scanning electron microscopy (cryo-SEM) furtherly. And it was also proved that the emulsion treated by proper HIU treatment at 300 W had better storage stability. Excessive HIU treatment (450 W, 600 W) had negative effects on the stability of emulsion. The stability of emulsion (300 W) against different environmental stresses was further explored, which established a theoretical basis for the industrial application of emulsion in food industry.     

Emulsion gels stabilized by soybean protein isolate and pectin: Effects of high intensity ultrasound on the gel properties,stability and β-carotene digestive characteristics

In this study, soybean protein isolate (SPI) and pectin emulsion gels were prepared by thermal induction, and the effects of high intensity ultrasound (HIU) at various powers (0, 150, 300, 450 and 600 W) on the structure, gel properties and stability of emulsion gels were investigated. Fourier transform infrared spectroscopy (FTIR) and X-ray diffraction (XRD) showed that the interaction between SPI and pectin was enhanced and the crystallinity of the emulsion gels was changed due to the HIU treatment. Confocal laser scanning microscopy (CLSM) and scanning electron microscopy (SEM) observations revealed that the particle size of the emulsion gels was decreased significantly by HIU treatment. The emulsion gel structure became more uniform and denser, which was conducive to storage stability. In addition, according to the low field nuclear magnetic resonance (LF-NMR) analysis, HIU treatment had no obvious impact on the content of bound water as the power increased to 450 W, while the content of free water decreased gradually and became immobilized water, which indicated that the water holding capacity of the emulsion gels was enhanced. Compared with untreated emulsion gel, differential scanning calorimetry (DSC) analysis showed that the denaturation temperature reached 131.9 ℃ from 128.2 ℃ when treated at 450 W. The chemical stability and bioaccessibility of β-carotene in the emulsion gels were improved significantly after HIU treatment during simulated in vitro digestion.     

Improvement of structural,physicochemical, and rheological properties of porcine myofibrillar proteins by high-intensity ultrasound treatment for application as Pickering stabilizers

This study aimed to evaluate the potential of time-dependent (0, 15, 30, 60, 120 min) treatment of porcine-derived myofibrillar proteins (MPs) with high-intensity ultrasound (HIU) for utilizing them as a Pickering stabilizer and decipher the underlying mechanism by which HIU treatment increases the emulsification and dispersion stability of MPs. To accomplish this, we analyzed the structural, physicochemical, and rheological properties of the HIU-treated MPs. Myosin heavy chain and actin were observed to be denatured, and the particle size of MPs decreased from 3,342.7 nm for the control group to 153.9 nm for 120 min HIU-treated MPs. Fourier-transformed infrared spectroscopy and circular dichroism spectroscopy confirmed that as the HIU treatment time increased, α-helical content increased, and β-sheet decreased, indicating that the protein secondary/tertiary structure was modified. In addition, the turbidity, apparent viscosity, and viscoelastic properties of the HIU-treated MP solution were decreased compared to the control, while the surface hydrophobicity was significantly increased. Analyses of the emulsification properties of the Pickering emulsions prepared using time-dependent HIU-treated MPs revealed that the emulsion activity index and emulsion stability index of HIU-treated MP were improved. Confocal laser scanning microscopy images indicated that small spherical droplets adsorbed with MPs were formed by HIU treatment and that dispersion stabilities were improved because the Turbiscan stability index of the HIU-treated group was lower than that of the control group. These findings could be used as supporting data for the utilizing porcine-derived MPs, which have been treated with HIU for appropriate time periods, as Pickering stabilizers.     

Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex

In this study, a soy protein isolate (SPI)-pectin (PC) complex was prepared, and the effects of different high intensity ultrasound (HIU) powers on the structure and solubility of the complex were studied. Fourier transform infrared (FTIR) spectroscopy analysis exhibited that with increasing HIU power, the α-helix content of the SPI in the complex was significantly reduced, and the random coil content increased; however, an opposite trend appeared after higher power treatments. Fluorescence spectra showed that HIU treatment increased the fluorescence intensity of the complex, and the surface hydrophobicity was increased. The trend of the protein structure studied by Raman spectroscopy was similar to that of FTIR and fluorescence spectroscopy. When the HIU treatment was performed for 15 min and at 450 W power, the particle size of the complex was 451.85 ± 2.17 nm, and the solubility was 89.04 ± 0.19 %, indicating that the HIU treatment caused the spatial conformation of the protein to loosen and improved the functional properties of the complex. Confocal laser scanning microscopy (CLSM) revealed that the complex after HIU treatment exhibited improved dispersibility in water and smaller particle size. Gel electrophoresis results indicated that HIU treatment did not affect the protein subunits of the complex. Therefore, the selection of a suitable HIU treatment power can effectively improve the structural properties and solubility of SPI in the complex, and promote the application of the SPI-PC complex in food processing and industries.     

Synergistic effect of preheating and different power output high-intensity ultrasound on the physicochemical,structural, and gelling properties of myofibrillar protein from chicken wooden breast

The effects of preheating to 50 ℃ and the subsequent application of high-intensity ultrasound (HIU, 20 kHz) at 200, 400, 600, and 800 W on the physicochemical, structural, and gelling properties of wooden breast myofibrillar protein (WBMP) were studied. Results suggested that the WBMP structure expanded to the balanced state at 600 W, and rheological properties exhibit that 600 W HIU (P < 0.05) significantly improved the storage modulus (G′) of WBMP. Notably, the WBMP gel (600 W) had the best hardness (65.428 ± 0.33 g), springiness (0.582 ± 0.01), and water-holding capacity (86.11 ± 0.83%). Raman spectra and low-field NMR indicated that 600 W HIU increased the β-fold content (37.94 ± 0.04%) and enlarged the immobilized-water proportion (93.87 ± 0.46%). Scanning electron micrographs confirmed that the gel was uniform and dense at 600 W. Therefore, preheating to 50 ℃ followed by HIU (600 W) helped form a superior WBMP gel.     

Solubilization and stable dispersion of myofibrillar proteins in water through the destruction and inhibition of the assembly of filaments using high-intensity ultrasound

The insolubility and poor dispersion of myofibrillar proteins (MPs) in water have always been the primary factors limiting the development of novel meat-based products. This study aimed to explore the mechanisms by which high-intensity ultrasound (HIU) at various power settings (0, 150, 300, 450 and 600 W) improved the solubility and dispersion stability of MPs in water. According to the solubility analysis, HIU significantly increased the water solubility of MPs (p < 0.05). The MPs treated with 450 W exhibited the best dispersion stability in water, which corresponded to the highest zeta-potential, smallest particle size and most uniform distribution (p < 0.05). Based on the circular dichroism and fluorescence spectroscopy and surface hydrophobicity analysis, the loss of the MP superhelix and subsequent random dissociation of the filamentous myosin structure appeared to be the main mechanism of MP solubilization. In addition, according to the zeta-potential, SDS-PAGE and Nano LC-ESI-MS/MS analyses, the increase in surface charge and the formation of soluble oligomers may provide additional forces to inhibit filament assembly, thereby improving the stability of the aqueous MP suspension. Atomic force microscopy (AFM) observations further confirmed these results. In conclusion, an HIU treatment effectively improves the solubility and dispersion stability of MP in water.     

Emulsions stabilised by casein and hyaluronic acid: Effects of high intensity ultrasound on the stability and vitamin E digestive characteristics

This study aimed to prepare an emulsion stabilised by an ultrasound-treated casein (CAS)-hyaluronic acid (HA) complex and to protect vitamin E during in vitro digestion. It was found that high-intensity ultrasound (HIU) treatment significantly changed the hydrogen bonding, electrostatic interaction and hydrophobic interaction between CAS and HA, reduced the particle size of the CAS-HA complex, increased the intermolecular electrostatic repulsion, and thus significantly improved the emulsifying properties of the CAS-HA complex. Meanwhile, the creaming index (CI) and confocal laser scanning microscopy images showed that the stability of the CAS-HA-stabilised emulsion was the best when treated at 150 W for 10 min, which could be attributed to the enhanced adsorption capacity of the CAS-HA complex at the oil–water interface and the viscosity of the formed emulsion. In vitro digestion experiments revealed that the emulsion stabilised by the ultrasound-treated CAS-HA complex had a good protective effect on vitamin E. This study is significant for the development of emulsions for the delivery of lipophilic nutrients.     

High-intensity ultrasound improves the physical stability of myofibrillar protein emulsion at low ionic strength by destroying and suppressing myosin molecular assembly

The specific molecular behavior of myofibrillar proteins (MPs) in low-salt media limits the development of muscle protein-based emulsions. This study aimed to evaluate the potential of high-intensity ultrasound (HIU; 150, 300, 450, and 600 W) to improve the physical stability of MP emulsion at low ionic strength and decipher the underlying mechanism. According to the physical stability analysis, HIU pretreatment, especially at 450 W power, significantly improved the physical stability of MP emulsions, as evidenced by the reduced particle size, enhanced inter-droplet interactions, and increased uniformity of the droplet size distribution (p < 0.05). The results of interfacial protein composition, Fourier transform infrared spectroscopy analysis, and microscopic morphology observation of the aqueous MP suspension suggested that HIU induced the depolymerization of filamentous myosin polymers and inhibited the subsequent self-assembly behavior. These effects may facilitate protein adsorption and molecular rearrangement at the oil–water interface, forming a complete interfacial layer and, thus, droplet stabilization. Confocal laser scanning microscopy observations further confirmed these results. In conclusion, these findings provide direct evidence for the role of HIU in improving the physical stability of MP emulsions at low ionic strength.     

Effect of high-intensity ultrasound on the technofunctional properties and structure of jackfruit (Artocarpus heterophyllus) seed protein isolate

The influence of high-intensity ultrasound (HIU) on the technofunctional properties and structure of jackfruit seed protein isolate (JSPI) was investigated. Protein solutions (10%, w/v) were sonicated for 15 min at 20 kHz to the following levels of power output: 200, 400, and 600 W (pulse duration: on-time, 5 s; off-time 1 s). Compared with untreated JSPI, HIU at 200 W and 400 W improved the oil holding capacity (OHC) and emulsifying capacity (EC), but the emulsifying activity (EA) and emulsion stability (ES) increased at 400 W and 600 W. The foaming capacity (FC) increased after all HIU treatments, as opposed to the water holding capacity (WHC), least gelation concentration (LGC), and foaming stability (FS), which all decreased except at pH 4 for FS. Tricine sodium dodecyl sulfate polyacrylamide gel electrophoresis (Tricine-SDS-PAGE) showed changes in the molecular weight of protein fractions after HIU treatment. Scanning electron microscopy (SEM) demonstrated that HIU disrupted the microstructure of JSPI, exhibiting larger aggregates. Surface hydrophobicity and protein solubility of the JSPI dispersions were enhanced after ultrasonication, which increased the destruction of internal hydrophobic interactions of protein molecules and accelerated the molecular motion of proteins to cause protein aggregation. These changes in the technofunctional and structural properties of JSPI could meet the complex needs of manufactured food products.     

Ultrasound-assisted gelation of β-carotene enriched oleogels based on candelilla wax-nut oils: Physical properties and in-vitro digestion analysis

This study investigated the effects of high-intensity ultrasound (HIU, 95 W, 10 s) on the physical properties, stability and in vitro digestion of β-carotene enriched oleogels. Candelilla wax (3 wt%) and nut oils (peanut, pine nut and walnut oil) with or without β-carotene were used to form oleogels. HIU improved the storage modules (G’) of peanut, pine nut and walnut oleogels without β-carotene from 11048.43 ± 728.85 Pa, 38111.67 ± 11663.98 Pa and 21921.13 ± 1011.55 Pa to 13502.40 ± 646.54 Pa, 75322.47 ± 9715.25 Pa and 48480.97 ± 4109.64 Pa, respectively. Moreover, HIU reduced oil loss of peanut, pine nut and walnut oleogels without β-carotene from 23.98 ± 2.58%, 17.14 ± 0.69% and 24.66 ± 1.57% to 17.60 ± 1.10%, 13.84 ± 0.74% and 18.72 ± 3.47%, respectively. X-ray diffraction patterns showed that HIU did not change the form of the crystal (β-polymorphic and β’-polymorphic) but increased the crystal intensity. Polarized light microscope images indicated that all oleogels showed more visible crystals after HIU. After 120 d of storage, HIU decreased the degradation of β-carotene for peanut oil and walnut oil samples (the contents of β-carotene in peanut and walnut oleogels without HIU after 120 d of storage were 897 ± 2 μg/g and 780 ± 1 μg/g, respectively, and those of sonicated samples were 1070 ± 4 μg/g and 932 ± 1 μg/g, respectively). Furthermore, HIU reduced the release of β-carotene in intestinal digestion. In conclusion, HIU could improve the functional properties of wax-nut oils oleogels and their β-carotene enriched oleogels.     

Synergistic modification of pea protein structure using high-intensity ultrasound and pH-shifting technology to improve solubility and emulsification

The most important factors restricting research and application in the food industry are the poor solubility and emulsification of pea protein isolate (PPI). This study investigates the effect of high-intensity ultrasound (HIU, 0–600 W) and pH-shifting treatment, alone or combined, on the structure, solubility, and emulsification of PPI, as well as its potential mechanism. The results revealed that the PPI solubility significantly increases when treated with the combination, corresponding to a decrease in the protein particle size, especially at 500 W of HIU power (p < 0.05). Correspondingly, the emulsion prepared from it was less prone to phase separation during storage. According to the structural analysis, the structural changes caused by protein unfolding (i.e., the exposure of hydrophobic and polar sites and the loss of the α-helix) seemed to be the primary reasons for increased PPI solubility. In addition, confocal laser scanning microscopy indicated that the combination treatment accelerated the adsorption of PPI at the oil/water interface and strengthened the compactness of the interface film. Improved interfacial properties and intermolecular forces played a critical role in the resistance to droplet coalescence in PPI emulsion. In conclusion, ultrasound and pH-shifting treatments have a synergistic effect on improving the solubility and emulsification of PPI.     

Ultrasonic structural modification of myofibrillar proteins from Coregonus peled improves emulsification properties

This study evaluated the effects of high intensity ultrasonication (HIU, 100, 150, 200, and 250 W) and treatment time (0, 3, 6, 9, and 12 min) on the structure and emulsification properties of myofibrillar proteins (MPs) from Coregonus peled. These investigations were conducted using an ultrasonic generator at a frequency of 20 kHz (ultrasonic probe). Analysis of the carbonyl content and total number of sulfhydryl groups showed that HIU significantly improved the oxidative modification of MPs (P < 0.05). SDS-PAGE profiling showed significant degradation of the myosin heavy chain (P < 0.05). In addition, Fourier transformed infrared spectroscopy (FTIR) revealed that HIU altered these treated MP secondary structures, this was due to molecular unfolding and stretching, exposing interior hydrophobic groups. Particle size analysis showed that HIU treatment reduced particle sizes. Solubility, emulsification capacity, and emulsion stability were improved significantly, and each decreased with an increase in treatment time (up to 12 min), indicating aggregation with prolonged sonication. These results indicate that HIU could improve the emulsification properties of MPs from C. peled, demonstrating a promising method for fish protein processing.     

Study on the emulsification and oxidative stability of ovalbumin-pectin-pumpkin seed oil emulsions using ovalbumin solution prepared by ultrasound

Pumpkin seed oil (PSO), which is a valuable compound with high nutritional value used for the prevention of various chronic diseases, is prone to oxidation. In this work, small and uniform (su) ovalbumin (OVA) and pectin (PEC) were used to stabilize PSO in the form of an emulsion. The results showed that suOVA-PEC-PSO emulsion with a droplet size of 9.82 ± 0.05 μm was successfully self-assembled from PSO, PEC, and suOVA solution (with a droplet size of 230.13 ± 14.10 nm) treated with 300 W ultrasound, owing to the formation of a more stable interfacial film on the surface of droplets. The interfacial, rheological, emulsifying, and antioxidant properties of the suOVA-PES-PSO emulsions were excellent, owing to the synergistic effects between PEC and suOVA solution. Moreover, the physical stability of the suOVA-PEC-PSO emulsions to salt stress, a freeze-thaw cycle, and heat treatment was also increased and the oxidation of linolenic acid was notably delayed. These results have extended the food-related applications of OVA and PSO, and provide a promising foundation for further exploration of the self-assembly of composite emulsions by small and uniform proteins.     

Post-mortem ultrasound and freezing of rabbit meat: Effects on the physicochemical quality and weight loss

High intensity ultrasound (HIU) is a technique with the potential to improve meat quality, however, more research is needed on its application within the chain of cold storage and freezing. This study evaluates the effect of HIU (40 kHz, 9.6 W/cm², 20 and 40 min) and post-mortem development on the yield and physicochemical quality of rabbit meat in samples treated with HIU pre- and post-storage in a freezer (120 h at −20 °C). Twenty rabbit carcasses were vacuum packed 12 h post-mortem, placed in a fridge at 4 °C for 24 h, and divided in two groups (HIU application before or after freezing), before assigning the treatments. The results show that HIU before freezing produced intense and bright orange-yellow colours, whereas its application after freezing resulted in pale red tones. HIU application accelerates rigor mortis resolution when it is applied before freezing and causes a significant decrease in pH immediately following the HIU treatment. Post-freezing application of HIU is not recommended because it considerably increased weight loss and toughening of the meat when long exposure times were used (40 min). In contrast, a short treatment duration with HIU mitigated the effects of freezing and produced significant increases in water-holding capacity (WHC) after cold storage. The yield (weight loss) of the rabbit meat was not affected when HIU was applied pre-freezing. The application of HIU pre-freezing constitutes a promising technology because it increased the tenderness and the WHC of rabbit meat. However, more research is needed to improve the appearance before scaling up to industrial levels.     

Effect of ultrasonic power on the stability of low-molecular-weight oyster peptides functional-nutrition W1/O/W2 double emulsion

Ultrasonic-assisted treatment is an eco-friendly and cost-effective emulsification method, and the acoustic cavitation effect produced by ultrasonic equipment is conducive to the formation of stable emulsion. However, its effect on the underlying stability of low-molecular-weight oyster peptides (LOPs) functional-nutrition W₁/O/W₂ double emulsion has not been reported. The effects of different ultrasonic power (50, 75, 100, 125, and 150 W) on the stability of double emulsions and the ability to mask the fishy odor of LOPs were investigated. Low ultrasonic power (50 W and 75 W) treatment failed to form a well-stabilized double emulsion, and excessive ultrasound treatment (150 W) destroyed its structure. At an ultrasonic power of 125 W, smaller particle-sized double emulsion was formed with more uniform distribution, more whiteness, and a lower viscosity coefficient. Meanwhile, the cavitation effect generated by 125 W ultrasonic power improved storage, and oxidative stabilities, emulsifying properties of double emulsion by reducing the droplet size and improved sensorial acceptability by masking the undesirable flavor of LOPs. The structure of the double emulsion was further confirmed by optical microscopy and confocal laser scanning microscopy. The ultrasonic-assisted treatment is of potential value for the industrial application of double emulsion in functional-nutrition foods.     

Effect of ultrasonic power on the emulsion stability of rice bran protein-chlorogenic acid emulsion

In this study, rice bran protein–chlorogenic acid (RBP–CA) emulsion was subjected to an ultrasonic-assisted treatment technique. The encapsulation efficiency and loading capacity of chlorogenic acid (CA), and the morphology, particle size, zeta (ζ)-potential, atomic force microscopy image, viscosity, turbidity, and interfacial protein content of the emulsion under different ultrasonic power were investigated. The results revealed that the emulsion exhibited an encapsulation efficiency and loading capacity of 86.26 ± 0.11% and 17.25 ± 0.06 g/100 g, respectively, at an ultrasonic power of 400 W. In addition, the size of the emulsion droplets decreased and became more evenly distributed. Furthermore, the viscosity of the emulsion decreased significantly, and it exhibited a turbidity and interfacial protein content of 24,758 and9.34 mg/m², respectively. Next, the storage, oxidation, thermal, and salt ion stabilities of the emulsion were evaluated. The results revealed that the ultrasonic-assisted treatment considerably improved the stability of the emulsion.     

Positive effects and mechanism of ultrasound on chitin preparation from shrimp shells by co-fermentation

The objective of this study is to explore the effect and mechanism of ultrasound on chitin extraction from shrimp shells powder (SSP) by the co-fermentation of Bacillus subtilis and Acetobacter pasteurianus. After pre-treating the SSP with high-intensity ultrasound (HIU) at 800 W, the protease activity in the fermentation solution reached 96.9 U/mL on day 3, which was significantly higher than for SSP that had not been pre-treated with ultrasound (81.8 U/mL). The fermentation time of the chitin extraction process was 5.0 d without ultrasound pre-treatment, while it was shortened to 4.5 d when using ultrasound at 800 W to treat SSP. However, there were no obvious differences when we applied ultrasound at low power (200 W, 400 W). Furthermore, chitin purified from shrimp shells pre-treated with HIU at 800 W exhibited lower molecular weight (11.2 kDa), higher chitin purity (89.8%), and a higher degree of deacetylation (21.1%) compared to SSP with no ultrasound pre-treatment (13.5 kDa, 86.6%, 18.5%). Results indicate that HIU peels off the protein/CaCO₃ matrix that covers the SSP surface. About 9.1% of protein and 4.7% of Ca²⁺ were released from SSP pre-treated with HIU at 800 W. These figures were both higher than with no ultrasound pre-treatment (4.5%, 3.2%). Additionally, the amount of soluble protein extracted from SSP through HIU at 800 W was 50% higher than for the control sample. SDS-PAGE analysis indicated that the soluble protein was degraded to the micromolecule. It also revealed that HIU (600, 800 W) induced the secondary and tertiary structure destruction of protein extracted from SSP. In conclusion, HIU-induced degradation and structural damage of protein enhances the protein/CaCO₃ matrix to be peeled off from SSP. Also, in the co-fermentation process, an increase of protease activity further accelerates deproteinization.     

Influence of sonication,temperature, and agitation,on the physical properties of a palm-based fat crystallized in a continuous system

High-intensity ultrasound (HIU) has been used in the past to change fat crystallization and physical properties of fat crystalline networks. The objective of this work was to evaluate how HIU placed on different positions in a scraped surface heat exchanger (SSHE) using different processing conditions affect the physical properties of an interesterified palm olein. The sample was crystallized at two temperatures (20 °C and 25 °C) and two agitation rates (344/208 rpm and 185/71 rpm, barrels/pin worker). HIU (12.7 mm-diameter tip, 50% amplitude, 5 s pulses) was placed at three different positions within the SSHE. After processing, samples were stored at 25 °C for 48 h and analyzed according to the crystal morphology, solid fat content (SFC), oil binding capacity (OBC), melting behavior, viscoelasticity, and hardness. Physical properties were affected by crystallization conditions, by sonication, and by HIU position. The greatest improvement obtained was at 20 °C using low agitation when HIU was placed at the beginning of the SSHE. These conditions result in a sample with 98.9% of OBC, 274 kPa of viscoelasticity and 31 N of hardness. These results show that HIU can be used as an additional processing tool to improve physical properties of a palm-based fat and that the best improvement was obtained as a combination of crystallization conditions and HIU position.     

Laccase cross-linking of sonicated α-Lactalbumin improves physical and oxidative stability of CLA oil in water emulsion

α-lactalbumin was modified by ultrasound (US, 20 kHz, 43 ± 3.4 W/cm⁻²) pre-treatments (0, 15, 30 and 60 min) and laccase cross-linking of sonicated α-lactalbumin was used to evaluate the physical and oxidative stability of conjugated linoleic acid (CLA) emulsions. The emulsions prepared with laccase cross-linking US-α-lactalbumin (α-lactalbumin treated with US pre-treatment) and US-α-lactalbumin were scrutinized for oxidative and physical stability at room temperature for two weeks of storage. Laccase cross-linking US-α-lactalbumin (Lac-US-α-lactalbumin) revealed improved physical stability in comparison with US-α-lactalbumin, specified by droplet size, structural morphology, adsorbed protein, emulsifying properties and creaming index. SDS-PAGE analysis showed that there was formation of polymers in Lac-US-α-lactalbumin emulsion. Surface hydrophobicity of Lac-US-α-lactalbumin was higher than that of US-α-lactalbumin, and gradually enhanced with the increase of ultrasound time. More importantly, the measurements of peroxide values and conjugated dienes were used to study the oxidative stability of the CLA emulsions. The Lac-US-α-lactalbumin emulsion proved to be reducing the synthesis of fatty acid hydroperoxides and less conjugated dienes compared to the native and US-α-lactalbumin emulsions. This study revealed that the combination of US pre-treatment and laccase cross-linking might be an effective technique for the modification of CLA emulsions.