Dynamic High-pressure Microfluidization Treatment Research Articles

Enhancing vitamin D3 bioaccessibility: Unveiling hydrophobic interactions in soybean protein isolate and vitamin D3 binding via an infant in vitro digestion model

In the domain of infant nutrition, optimizing the absorption of crucial nutrients such as vitamin D3 (VD3) is paramount. This study harnessed dynamic-high-pressure microfluidization (DHPM) on soybean protein isolate (SPI) to engineer SPI-VD3 nanoparticles for fortifying yogurt. Characterized by notable binding affinity (Ka = 0.166 × 105 L·mol−1) at 80 MPa and significant surface hydrophobicity (H0 = 3494), these nanoparticles demonstrated promising attributes through molecular simulations. During simulated infant digestion, the 80 MPa DHPM-treated nanoparticles showcased an impressive 74.4% VD3 bioaccessibility, delineating the pivotal roles of hydrophobicity, bioaccessibility, and micellization dynamics. Noteworthy was their traversal through the gastrointestinal tract, illuminating bile salts' crucial function in facilitating VD3 re-encapsulation, thereby mitigating crystallization and augmenting absorption. Moreover, DHPM treatment imparted enhancements in nanoparticle integrity and hydrophobic properties, consequently amplifying VD3 bioavailability. This investigation underscores the potential of SPI-VD3 nanoparticles in bolstering VD3 absorption, thereby furnishing invaluable insights for tailored infant nutrition formulations.

Effect of dynamic high-pressure microfluidization treatment on soybean protein isolate–rutin non-covalent complexes

In this investigation, soybean protein isolate–rutin (SPI–RT) complexes were treated using dynamic high-pressure microfluidization (DHPM). The effects of this process on the physicochemical and thermodynamic properties of SPI were investigated at different pressures. Fourier-transform infrared spectroscopy and fluorescence spectroscopy provided evidence that the SPI structure had been altered. The binding of SPI to RT resulted in a decrease in the percentage of α-helices and random curls as well as an increase in the percentage of β-sheets. In particular, the α-helix content decreased from 29.84 % to 26.46 %, the random curl content decreased from 17.45 % to 15.57 %, and the β-sheet content increased from 25.37 % to 26.53 %. Moreover, fluorescence intensity decreased, and the emission peak of the complex was red-shifted by 6 nm, exposing the internal groups. Based on fluorescence quenching analysis, optimal SPI–RT complexation was achieved after 120-MPa DHPM treatment, and molecular docking analysis verified the interaction between SPI and RT. The minimum particle size, maximum absolute potential, and total phenolic content of the complexes were 78.06 nm, 21.4 mV and 74.35 nmol/mg protein, respectively. Furthermore, laser confocal microscopy revealed that the complex particles had the best microstructure. Non-covalent interactions between the two were confirmed using sodium dodecyl sulfate–polyacrylamide gel electrophoresis. Moreover, the hydrophobicity of the complex particle's surface increased to 16,045 after 120-MPa DHPM treatment. The results of this study suggest that DHPM strongly promotes the improvement of the physicochemical properties of SPI, and provide a theoretical groundwork for further research.

Microfluidization of soybean protein isolate-tannic acid complex stabilized emulsions: Characterization of emulsion properties, stability and in vitro digestion properties

Emulsion stability and sustained-release can be improved with a non-covalent complexing of a soybean protein isolate (SPI) with -tannic acid (TA) and dynamic high-pressure microfluidization (DHPM). The microstructure, physicochemical properties, and interfacial properties were investigated. The properties of the DHPM-treated emulsions were improved significantly, with the 120 MPa DHPM-treated SPI-TA emulsion (SPI-TA 120) having the best microstructure. The highest interface protein content, viscosity and viscoelasticity at 120 MPa of pressure facilitated the stability of the emulsion. The oxidation kinetics of emulsions was established. It was demonstrated that the oxidation stability of SPI-TA 120 was higher than SPI and SPI-TA emulsions without DHPM treatment. In addition, DHPM-treated SPI-TA emulsions showed the most positive effect on the slow release of curcumin compared to the control group. The formation of non-covalent protein complexes with polyphenols and DHPM treatment effectively increases the stability of emulsions.

Dynamic high-pressure microfluidization assist in stabilizing hemp seed protein-gum Arabic bilayer emulsions: Rheological properties and oxidation kinetic model

Hemp seed protein (HSP) stabilized emulsion was subjected to dynamic high-pressure microfluidization (DHPM). Gum Arabic (GA) was added to the emulsion system to prepare HSP-GA bilayer emulsion, which improved the stability of hemp seed oil (HSO). Under the DHPM treatment at 120 MPa, the particle size of HSP-GA bilayer emulsion was 260.02 nm and the zeta potential was − 25.9 mV. The interfacial adsorbed protein of the DHPM-treated emulsion increased to 37.35%. And the viscosity, the storage modulus (G'), and loss modulus (G") were increased. The HSP-GA emulsion under 120 MPa was selected to develop an oxidation kinetic model to obtain equation c=e10.56086e−3659.66658T*t+0.72, which was used to predict the POV variation of HSO within the bilayer emulsion system. The CBD retention rate was 93.54% during storage for 20 days. It can be concluded that the effective encapsulation of DHPM treatment and bilayer emulsion system is beneficial to broaden the application of hemp seeds in processing industry.

Effect of dynamic high-pressure microfluidization on physicochemical, structural, and functional properties of oat protein isolate

Dynamic high-pressure microfluidization (DHPM) technology was used to treat oat protein isolate (OPI) to improve its functional properties and broaden its application in food processing. Results showed that the particle size of OPI was significantly reduced by 70.96%, and the absolute zeta potential increased by 33.51% at a DHPM pressure of 120 MPa. The major subunits of OPI were not degraded, but the secondary structures of OPI were altered with increasing α-helix, β-sheet, and β-turn structures and decreasing random coil after DHPM treatment. In addition, the significant increase in the surface hydrophobicity and free sulfhydryl content, as well as fluorescence quenching of OPI indicated the conformational expansion and rearrangement of OPI. Additionally, the changes in OPI structures affected its functional performance. DHPM treatment at 120 MPa significantly improved the solubility, water and oil holding properties, and emulsifying and foaming abilities of OPI. Therefore, DHPM treatment can improve the functional properties of OPI, which provides a new idea for expanding the application of OPI in food processing.

Dynamic high‐pressure microfluidization enhanced the emulsifying properties of wheat gliadin by rutin

Dynamic high-pressure microfluidization (DHPM) has attracted increasing interest in food macromolecule modification, which has been used in the preparation of nanoemulsions, gel-like soy protein emulsions, and nanocelluloses. This study explored the effects of DHPM under 0, 40, 80, 120, and 160 MPa with the addition of rutin on the physical, structural, rheological, and morphological characteristics of wheat gliadin. Infrared spectrum analysis showed that the DHPM treatment resulted in the structural changes of wheat gliadin and the primary interactions between wheat gliadin and rutin were hydrogen bond and hydrophobic effects. Here, 120 MPa DHPM treatment with the addition of rutin caused decreased particle sizes but increased zeta-potential and viscoelastic properties of wheat gliadin, with particle sizes at 245.20 nm and zeta-potential at 21.76 mV, respectively. The results showed that the combination of DHPM treatment at 120 MPa and rutin to wheat gliadin exhibited the morphology of nanospheres with a more compact structure, uniform particle distribution, and fine emulsifying properties. Practical applications The interaction between protein and polyphenol are able to preserve the stability of the functional compounds, allow targeted and controlled release, improve texture in the food industry. Improvement of functional characteristics of protein-polyphenol complexes with high emulsifying stability during food processing is crucial to use in the food industry. Therefore, the goal of this research is to use a soluble complex of gliadin-rutin for the development of its functional characteristics.

In vitro digestion and structural properties of rice starch modified by high methoxyl pectin and dynamic high-pressure microfluidization

The rheological, structural properties and in vitro digestibility of starch with high methoxyl pectin (HMP) and further modified by dynamic high-pressure microfluidization (DHPM) were investigated. The viscosity and elasticity increased on addition of HMP and were more pronouncedly affected by 10% HMP. However, after DHPM treatment, the viscosity and elasticity decreased with increasing DHPM pressure. After 100 MPa DHPM treatment, the ordered and crystalline structures were further increased compared with starch–HMP mixtures. A compact and dense surface of starch paste was formed under 100 MPa DHPM and 10% HMP treatment, thus significantly slowing down the digestibility. In contrast, the crystalline and semicrystalline structure of starch were disrupted by intense shear force under 200 MPa DHPM. This study provides theoretical information regarding starch–HMP interaction and improves their functional and physicochemical properties through a promising strategy for better applications in food formulation.

Modulation of the structural and functional properties of perilla protein isolate from oilseed residues by dynamic high-pressure microfluidization

Dynamic high-pressure microfluidization (DHPM) is an alternative method to physically modify proteins to improve their functional properties. In this study, perilla protein isolate (PPI) was treated by DHPM at different pressures. Results showed that DHPM treatment reduced the particle size and absolute potential of PPI by 75.90% and 22.28%. The increased surface hydrophobicity and free sulfhydryl content were observed in DHPM-treated PPI, which may be caused by the comformation changes of PPI. Furthermore, DHPM treatment would not cause the degradation of the main subunits and the variation of crystalline regions in PPI, but enhancing the thermal stability of PPI at 90 MPa and 120 MPa. Functional properties analysis indicated that DHPM treatment at 120 MPa was more effective in improving the solubility, foaming and emulsifying capacities of PPI. The results suggested that DHPM can be used to enhance the functional properties of PPI and expand its application in food systems.

Effects of dynamic high-pressure microfluidization on the physicochemical, structural and functional characteristics of Eucommia ulmoides Oliv. seed meal proteins

Eucommia ulmoides Oliv. seed oil byproducts are rich in edible proteins (35.98%, dry matter) and have been scarcely investigated. Therefore, E. ulmoides seed meal proteins (ESMPs) were extracted and modified by dynamic high-pressure microfluidization (DHPM). The results showed that DHPM induced an increase in the α-helix to β-sheet ratio of ESMPs, implying the enhancement of ESMPs bioavailability. The average particle size and absolute zeta potential of ESMPs were significantly (p < 0.05) reduced by 91.07% and 27.88%, respectively, with pressure rising to 160 MPa. The solubility of ESMPs via DHPM treatment was noticeably (p < 0.05) increased. DHPM treatment elevated the water holding capacity of ESMPs under acidic conditions as well as the fat absorption capability under high temperature. The foaming properties of ESMPs depended on the protein concentration and DHPM treatment. DHPM at 40, 80, and 120 MPa significantly improved (p < 0.05) the emulsifying capability of ESMPs. Therefore, DHPM treatment would be promising for modifying the functional characteristics of ESMPs.

Gel properties and structural characteristics of soy protein isolate treated with different salt ions before spray drying combined with dynamic high-pressure micro-fluidization

The gelation properties of soy protein isolate (SPI) were influenced by the addition of salt ions (SI) before spray drying combined with dynamic high-pressure microfluidization (DHPM). Compared with SPI, SPI treated using SIDHPM (SIDHPM-SPI) markedly increased in gel hardness, springiness, cohesivenessand chewiness upon heating (p < 0.05). The changes were mainly attributable to buried functional groups coming to the surface with DHPM treatment, which improved the interactions between protein molecules. FT-IR spectroscopy indicated that the SIDHPM treatment resulted in the conversion of SPI α-helix, β-turns and random coil to β-sheet structures. The analysis of the intermolecular interaction forces indicated that disulfide bonds and hydrophobic interactions were the critical molecular forces in maintaining the gel network structure. Compared with SPI, SIDHPM-SPI increased the water-holding capacity of gels. Analysis using scanning electron microscopy indicated that modification using SIDHPM allowed the formation of SPI gels with a continuous and homogeneous gel complex configuration. Moreover, the sensory evaluation of the SIDHPM gels was consistent with the results of the instrumental analysis. Thus, SIDHPM led to a gel product with better overall performance, which might potentially be used to fabricate SPI with improved functionality for use by the food industry.

Effects of dynamic high-pressure microfluidization treatment on the functional and structural properties of potato protein isolate and its complex with chitosan

In our previous work, dynamic high-pressure microfluidization (DHPM) treatment was shown to promote the interaction between chitosan (CS) and potato protein isolate (PPI), but the modification mechanism of DHPM treatment (6 k–12 k psi) on PPI and its complex with CS remains to be elucidated. Here, moderate DHPM treatment (≤9k psi) was found to decrease the particle size, increase the surface charge, and improve the solubility of PPI and its emulsifying and foaming properties. The PPI functional properties were further improved by CS addition followed by DHPM treatment. The ultraviolet and fluorescence spectral results showed that DHPM treatment could destroy the PPI molecularstructure, while CS addition could provide a protective mechanism against PPI damage, which was also proved by the surface hydrophobicity. The circular dichroism spectral analysis exhibited that DHPM treatment could convert different types of secondary structures by disrupting the PPI intermolecular hydrogen bonds, while CS addition could promote the formation of hydrogen bonds in the system, which was also demonstrated by infrared spectroscopy. The sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) results exhibited that DHPM treatment (≤12 k psi) was not sufficient to reduce the PPI molecular mass, while DHPM treatment (6 k-12 k psi) could destroy the structure of CS/PPI complex. The thermodynamic analysis showed that the PPI thermodynamic stability could be improved by DHPM treatment, but decreased by CS addition plus DHPM treatment. These results showed that DHPM treatment has a good potential to modify the PPI and CS/PPI complex.

Effect of dynamic high pressure microfluidization treatment on physical stability, microstructure and carotenoids release of sea buckthorn juice

During the sea buckthorn juice production, poor physical stability and loss of bioactive substances will reduce the nutritional and commodity value of product. In this study, the sea buckthorn juice was subjected to dynamic high pressure microfluidization (DHPM) treatment with different pressures (50, 75, 100, 125, and 150 MPa) and different passes (1, 2 and 3). The effect on physical and chemical indexes of juice was investigated. Results indicated that the particle size of all the treated samples became smaller (p < 0.05) compared with control, but the D[4,3] became larger in sea buckthorn juice with increasing passes number of homogenization. Besides, physical stability analysis suggested that DHPM was beneficial to improving the stability of the juice. Regarding to carotenoids content, when the samples were treated at 150 MPa for one and two passes, there were no significant changes in total carotenoids content compared with the control. In addition, it was also observed that no significant changes in α-carotene (except treated at 100 MPa) and β-carotene. The results provide a basis for the improvement of sensory and nutritional quality, and the improvement of stability and bioavailability of carotenoids in sea buckthorn juice.

Effect of dynamic high pressure microfluidization on the solubility properties and structure profiles of proteins in water-insoluble fraction of edible bird's nests

In this study, water-insoluble fraction of edible birds' nest (EBN) was treated with dynamic high pressure microfluidization (DHPM) under 40, 80, 120, and 160 MPa of pressure. The results displayed a remarkable pressure-related increase in protein solubility upon DHPM treatment. In addition, circular dichroism spectra also revealed that DHPM treatment induced conformational changes such as increase in α-helix and β-turn, whereas intrinsic fluorescence spectroscopy showed that tryptophan residues were less exposed to solvent. Furthermore, the increased surface hydrophobicity accompanied by reduced particle size was observed in DHPM treated samples, which was in good agreement with results of atomic force microscopy analysis, showing de-aggregation of large proteins in EBN water-insoluble fraction. Hence, our study shows that DHPM treatment can solubilize proteins from EBN water-insoluble fraction, and is an alternative method to traditional stewing to release the functional ingredients from EBN insoluble fraction, which can be introduced into industrial EBN food processing.

The anti-lipidemic role of soluble dietary fiber extract from okara after fermentation and dynamic high-pressure microfluidization treatment to Kunming mice.

The present study was conducted to evaluate the anti-hyperlipidemia ability of the dietary fiber extracted from okara in mice fed a high cholesterol diet. The dietary fiber was extracted from okara by combining fermentation with dynamic high-pressure microfluidization. An animal model was established to test the hypothesis that soluble dietary fiber, insoluble dietary fiber and total dietary fiber inhibit the fatty liver could be related to the total lipids and cholesterol including total cholesterol, triglyceride, low-density lipoprotein cholesterol and high-density lipoprotein cholesterol in the serum. Compared with mice fed with simvastatin, mice fed dietary fiber can significantly reduce their serum total cholesterol, low-density lipoprotein cholesterol, triglyceride, and atherogenic index whereas no significant effect on high-density lipoprotein cholesterol was observed. Dietary fiber lowered a high level of liver total cholesterol and triglyceride. The dietary fiber extracted from okara might play an important role in the prevention of hyperlipidemia in high cholesterol mice and could be used as a natural supplement to a high cholesterol diet of functional food, due to the suppression of liver lipid synthesis.

The formation mechanism and thermodynamic properties of potato protein isolate–chitosan complex under dynamic high-pressure microfluidization (DHPM) treatment

The objective of the study was to explore the formation mechanism and thermodynamic properties of chitosan (CS)–potato protein isolate (PPI) complex under DHPM treatment. The transmission electron microscopic (TEM) results showed the formation of a complex between CS and PPI. Meanwhile, particle size and zeta-potential were shown to increase with increasing CS concentration, further confirming the formation of the complex. The surface hydrophobicity results showed CS was bound to PPI by hydrogen bond. The ultraviolet and fluorescence spectral analysis exhibited CS formed a protective mechanism against PPI destruction, preventing the exposure of tyrosine and tryptophan residues. Infrared spectrum and circular dichroism spectral analysis revealed no occurrence of chemical reaction between CS and PPI under DHPM treatment, further indicating that they are bound by hydrogen bond and hydrophobic interaction. Moreover, CS addition was shown to enhance the intermolecular interaction and promote the formation of intermolecular hydrogen bond network. Differential scanning calorimetry (DSC) and thermo gravimetric analysis (TGA) revealed that CS addition could improve the thermal stability of PPI. These results have shed light on the formation mechanism and thermodynamic properties of the CS/PPI complex and facilitate its application in food industry.

Different aggregation states of barley β-glucan molecules affects their solution behavior: A comparative analysis

Barley β-glucan (BBG) is of admirable health advantages, the physiochemical and functional properties of BBG might be affected by its extraction process. The new high speed centrifugal-vortex extraction method was compared to a traditional method, and the extracted BBG was treated by dynamic high-pressure microfluidization (DHPM) to analysis the effect of the extraction and DHPM on molecular weight (MW), solution behavior and structural features of BBG. The new method reduced the extraction time by half, increased the yield by about 10%. The DHPM treatment made the BBG viscosity lower and the aggregation particle size distribution narrower. Although the molecular weight was reduced by DHPM treatment, the FT-IR and microstructure results showed that the exogenous physical treatment did not change the primary structure. These results indicated that the solution behavior of BBG affected by exogenous physical treatment was due to the changes of intermolecular aggregation states and high-level structure of BBG molecules.

Reduced IgE/IgG binding capacities of bovine α-Lactalbumin by glycation after dynamic high-pressure microfluidization pretreatment evaluated by high resolution mass spectrometry

Dynamic high-pressure microfluidization (DHPM) pretreatment and glycation with lactose were employed to modify α-Lactalbumin (α-LA) with respect to the IgE/IgG binding capacities. No significant difference on incorporation ratio value of glycated α-LA was observed with and without DHPM pretreatment. However, IgE/IgG binding capacities of α-LA were decreased after glycation and DHPM pretreatment promoted the reduction. The lowest IgE/IgG binding capacities of glycated α-LA were obtained by DHPM pretreatment at 110 MPa. Native α-LA was mainly glycated at K62, K94, K98, whereas glycation sites and degree of substitution per peptide (DSP) were added after DHPM treatment. Therefore, the reduced IgE/IgG binding capacities of α-LA was attributed to the characteristics of glycated sites, including the amount, location, and DSP values. Interestingly, K98 played the most important role in decreasing IgE/IgG binding capacities of α-LA. The study revealed that glycation combined with DHPM was a promising way to decrease the allergenicity of proteins.

Dynamic High-Pressure Microfluidization-Treated Pectin under Different Ethanol Concentrations.

We previously reported that dynamic high-pressure microfluidization (DHPM) can degrade pectin in aqueous solution. In this study, we further investigated the effect of DHPM on pectin in water-ethanol systems. In the absence of DHPM treatment, it was found that pectin exhibited increased average particle size and unchanged average molecular weight, but a decline in reducing-sugar-ends content with the increase of ethanol concentrations (0–10% v/v). These results indicated that the addition of ethanol induced aggregation of pectin. During DHPM treatment, pectin underwent disaggregation and degradation under all measured ethanol concentrations. Disaggregation was enhanced but degradation was weakened with the increase of ethanol concentration. FT-IR and UV spectra indicated that demethylation but no β-elimination occurred in the water-ethanol system during DHPM. Finally, the mechanism of DHPM-induced disaggregation and degradation of pectin under a water-ethanol system was updated. This work may help us to find a suitable condition for reducing the degradation of pectin during the process of homogenization.

Comparison of antigenicity and conformational changes to β-lactoglobulin following kestose glycation reaction with and without dynamic high-pressure microfluidization treatment

Previous work indicated that conformational changes of β-lactoglobulin (β-LG) induced by dynamic high pressure microfluidization (DHPM) was related to the increase of antigenicity. In this study, β-LG glycated with 1-kestose and combined with DHPM decreased the antigenicity of β-LG. The antigenicity of control, β-LG-kestose (0.1 MPa) and β-LG-kestose (80 MPa) were 100, 79 and 42 μg/mL respectively. The molecular weight of β-LG conjugated to kestose increased from 18.4 to 19.6 kDa and its conformation scarcely changed. Conversely, combined with DHPM treatment (80 MPa), β-LG conjugated to kestose formed two conjugates with molecular weight of 18.8 and 19.8 kDa, respectively. Furthermore, the unfolding of β-LG as a result of the treatments is reflected by a decrease of intrinsic and synchronous fluorescence intensity and changes to the secondary structure. The conformational changes induced by DHPM and glycation treatments synergistically decrease the antigenicity of β-LG due to more masked or disrupted epitopes.

Antigenicity of β-lactoglobulin reduced by combining with oleic acid during dynamic high-pressure microfluidization: Multi-spectroscopy and molecule dynamics simulation analysis

Some food components can modulate the antigenicity of β-lactoglobulin (β-LG). This study investigated the role of oleic acid (OA) in reducing the antigenicity of β-LG. The results indicate the antigenicity of β-LG gradually decreased from 15 (sample with no OA) to 9.86, 7.51, and 6.01 µg/mL when interacting with OA during dynamic high-pressure microfluidization treatment at 0.1, 80, and 160 MPa. Although binding sites (n) of β-LG combined with OA at 0.1, 80, and 160 MPa decreased from 0.79 to 0.5 and 0.66, β-LG had a higher binding affinity (Ka) to OA than that of untreated β-LG. The values of Ka for β-LG/OA at 0.1, 80, and 160 MPa were 5.51 × 106, 17.43 × 106, and 49.75 × 106M-1, respectively. The molecule dynamic simulation showed that the OA molecules located at both β-barrel (site 1) interacted with Lys60, Glu62, and Lys69 and outer surface site 2 consisting of Tyr20, Tyr42, Ser21, Glu157, and His161. Additionally, when binding with OA during the dynamic high-pressure microfluidization treatment, the conformation of β-LG changed, reflected by the decrease of fluorescence intensity and total sulfhydryl group content, the increase of surface sulfhydryl group content, and secondary structure changes of β-LG. These results deduce that some epitopes may be masked by OA or modified by the conformational changes, resulting in the decline of antigenicity of β-LG molecules.