Effect Of High Pressure Homogenization Research Articles

Structural, properties and digestion in vitro changes of starch subjected to high pressure homogenization: An update review.

High pressure homogenization (HPH) is considered as a promising method for improving the ideal metabolic reaction of starch-based foods in the body, but there is still no comprehensive understanding of the structure-property relationship of starch treated with HPH. This study reviews the advantages and limitations of HPH in starch-based foods processing in recent years. It also elaborates the bidirectional regulation of HPH on starch structure-property and its potential in improving nutritional quality, which includes the regular modification effects of HPH on the multi-scale structure, physicochemical properties, and digestion characteristics of starch. It was found that HPH could lead to the degradation of amylopectin, destruction of amorphous structure, and homogenization of fine particles, promoting gelatinization and ultimately endowing starch with good solubility and digestibility. Moreover, it could reorganize and reorder the internal starch chains, or cause the particles to disintegrate into an amorphous state, thereby enhancing the anti-digestibility of starch. The interaction of starch with different nutrients during the HPH process could be further investigated in future studies and explored with other techniques for structure-property modifications, which would help expand the development of personalized starch foods to meet growing consumer demands.

Effects of High-Pressure Homogenization on the Structure and Functional Properties of Solenaia oleivora Proteins.

Solenaia oleivora, a rare freshwater shellfish with high protein quality, is unique to China. However, the poor hydrosolubility and functional properties of Solenaia oleivora proteins hinder their utilization in food products. Herein, the alkaline dissolution-isoelectric precipitation method was used for the extraction of Solenaia oleivora proteins. Furthermore, the impact of high-pressure homogenization (HPH) treatment varying from 0 to 100 MPa on the structure and functional properties of Solenaia oleivora proteins was investigated. The obtained results indicated that HPH treatment decreased the α-helix content and enhanced the β-sheet and random coil content. Furthermore, the HPH caused the unfolding of protein structure, exposing aromatic amino acids, increasing the free thiol group content, and enhancing surface hydrophobicity. As the homogenization pressure increased from 0 to 100 MPa, the particle size of Solenaia oleivora proteins decreased from 899 to 197 nm with the polymer dispersity index (PDI) value decreased from 0.418 to 0.151, the ζ-potential increased from -22.82 to -43.26 mV, and the solubility increased from 9.54% to 89.96%. Owing to the significant changes in protein structure and solubility, the emulsifying, foaming, and digestive properties of Solenaia oleivora proteins have been significantly improved after treatment with HPH.

Application of high-pressure homogenization-assisted pH-shift to enhance techno-functional and interfacial properties of lentil protein isolate

High-pressure homogenization (HPH) is a promising physical non-thermal approach to improve protein techno-functionality. This study aims to examine the effects of HPH on the lentil proteins through the perspective of the interfacial adsorption mechanism. The impact of HPH treatment on lentil protein isolate (LPI) at varying pressure levels (0–150 MPa) was determined using several analytical techniques, including SDS-PAGE, FTIR, solubility, and techno-functional properties (foaming and emulsifying properties), alongside analyses of interfacial tension and interfacial shear rheology at the o/w and a/w interfaces for two pH values (2.0 and 4.5). Results reveal that HPH treatment up to 100 MPa effectively unfolds lentil proteins by disrupting disulfide-bonded subunits into lower molecular weight fractions and unfolding highly-ordered secondary structures into random coils. LPI's capacity to produce emulsions and foams was found to be enhanced concurrently with these physicochemical changes, particularly at pressures up to 50 MPa. The findings aligned with the interfacial tension and shear rheology analyses, which show that proteins can form interfacial viscoelastic films on both o/w and a/w interfaces. Furthermore, the interfacial behavior of LPI and the effect of HPH on the interfacial behavior were found to be pH-dependent. The lower interfacial tension and the higher interfacial viscoelastic moduli (G′ and G″) were recorded at 50 MPa and 0 MPa at pH 2.0 and 4.5, respectively. These results stated that the effects of the HPH on the technofunctionality of LPI can be further enlightened by investigating the interfacial adsorption kinetics.

Development and characterization of pH-sensing films based on red pitaya (Hylocereus polyrhizus) peel treated by high-pressure homogenization for monitoring fish freshness

High pressure homogenization (HPH) was used to physically modify red pitaya (Hylocereus polyrhizus) peel (RPP) dispersions to develop pH-sensing films for monitoring fish freshness. Effects of HPH treatment at various pressures of 0 (control), 10, 20, 30, 40, 60 and 80 MPa on microstructure and properties of RPP film-forming dispersions (FFDs) and their resultant films were systematically investigated. Results showed that due to the structure destructing effect of HPH, the mean particle size of RPP dispersion treated at 80 MPa decreased significantly from 129.17 to 37.41 μm and its total soluble solids content increased from 7.64 to 8.62 °Bx. Rheological analysis manifested that all FFDs exhibited a shear thinning behavior with higher apparent viscosities as well as storage modulus and loss modulus with increasing HPH pressure. Besides, the HPH treated FFDs had a higher total betacyanins content and showed an obvious color response to pH variation. Consequently, the resultant films had not only smoother surfaces and more transparent appearance, but also better water vapor barrier and mechanical properties than the control. Particularly, film obtained from RPP treated at 60 MPa showed a highest tensile strength of 21.87 MPa and elongation at break of 22.09%, together with a lowest water vapor permeability of 11.41 g⋅mm⋅m−2⋅d−1⋅kPa−1. Notably, this film also exhibited high sensitivity to volatile ammonia and showed a remarkable color variation when applied for monitoring fish spoilage at 25 °C. Thus, the pH-sensing films developed from HPH treated RPP had desirable properties to be potentially used in intelligent food packaging.

Effect of high-pressure homogenization on maize starch-stearic acid and maize starch-stearic acid-whey protein complexes

The maize starch (MS)-stearic acid (SA) and MS-SA-whey protein (WP) complexes were prepared using the high-pressure homogenization (HPH). Results from X-ray diffraction (XRD) showed that MS-SA complexes presented an increase in the long-range molecular order with increasing the homogenization pressure, and MS-SA-WP complexes showed only an increase with increasing the homogenization pressure from 10 to 50 MPa. Results from differential scanning calorimetry (DSC) and Raman spectroscopy showed that the amount of complexes and the short-range order of both MS-SA and MS-SA-WP complexes increased with increasing the homogenization pressure. The addition of WP to MS-SA altered significantly the structure and digestion of complexes. Results revealed that MS-SA-WP complexes have more ordered structure and lower digestion than the corresponding MS-SA complexes. The digestibility of all complexes decreased with increasing the homogenization pressure. There was a significant correlation between the digestibility and structural characteristics of complexes. Complexes with better structural stability have better anti-digestion properties. The obtained results are helpful in understanding the structure and digestibility of complexes prepared by HPH, which is valuable for controlling the quality and nutrition of starchy food.

Effect of High-Pressure Homogenization on the Properties and Structure of Cold-Induced Chiba Tofu Gel in Soy Protein Isolate.

In the actual production process of soy protein isolate (SPI), most of the homogeneous operating pressure is controlled below 20 MPa due to the consideration of production safety and the limitation of the pressure control capability of homogeneous equipment. In order to improve the functional properties of SPI and adapt it to actual production, the effects of different homogeneous pressures (4, 8, 10, 12, and 14 MPa) on the structure and gel properties of SPI were studied from the perspective of production control. Compared to the control group, the modified SPI improved the hardness, springiness, cohesiveness, chewiness, and water holding capacity (WHC) of the protein gel (p < 0.05). Rheological analysis shows that both G' and G″ increase with increasing frequency, reaching a maximum at 12 MPa. The gel intermolecular force results show that the disulfide bond, hydrophobic interaction, and non-disulfide bond are important molecular forces for gel formation. The particle size distribution uniformity of modified SPI was high, and scanning electron microscopy (SEM) analysis showed that the protein gel with a continuous uniform and dense network structure could be formed by high-pressure homogeneous modification. Overall, high-pressure homogenization technology has the potential to improve SPI gel structure and WHC, and 12 MPa modified SPI gel has the most significant effect.

Effect of high pressure homogenization on in vitro digestibility and colon fermentability of pea protein-rich bread designed for elderly consumers.

Enrichment of staple foods with proteins can be a solution to tackle protein-energy malnutrition in the elderly. For instance, bread can be enriched with pea proteins that are cheap, sustainable and easily digestible. Non-conventional technologies, such as high pressure homogenization (HPH), can improve the digestibility of plant proteins. To characterize the health functionality of pea-enriched bread, a functional bread tailored to elderly consumers was developed by substituting 5% wheat flour with untreated or HPH-treated pea protein concentrate. Protein digestibility and colon fermentability were assessed by mimicking elderly in vitro gastrointestinal and gut microbiota conditions and compared with adult conditions. Bread reformulation with pea proteins affected physical and chemical properties and produced an increase in hardness, which is one of the key features for the acceptability of bread by the elderly. The highest hardness value was observed for pea protein bread, followed by HPH-treated pea protein bread and wheat bread. In vitro protein digestibility and fermentability were affected by reformulation and by physiological digestive conditions, with lower digestibility under elderly conditions compared to adult ones. The obtained results may contribute to a better understanding of food digestibility under different gastrointestinal conditions and its dependence on physiological and formulation factors, and ultimately would help to design age-tailored foods.

Effect of High-Pressure Homogenization and Fat Content on Yogurt Fermentation Process

Effect of High-Pressure Homogenization and Fat Content on Yogurt Fermentation Process

Structure, bioavailability and physicochemical properties of icariin-soymilk nanoparticle

Soymilk is a natural nanocarrier. However, the performance of flavonoid-soymilk nano-complex remains unclear. In this work, icariin-soymilk nano-complexes (ISNCs) were successfully fabricated and characterized. The effects of high-pressure homogenization (HPH) treatment on structure and physicochemical properties of soymilk and nano-complexes were investigated. HPH treatment could significantly improve the surface hydrophobicity and interfacial activity of soymilk. The soymilk with HPH treatment could significantly improve the water solubility (20 folds), thermal stability and bioavailability of icariin. The highest encapsulation efficiency (93.28 %), loading capacity (39.09 µg/mg), ζ-potentia (absolute value, 31.20 mV) and bioavailability (72.14 %) were observed in HSI-200 (200 bar of homogenization pressure). While HSI-500 (500 bar of homogenization pressure) showed the smallest particle size (183.73 nm). ISNCs showed a rougher surface and an irregular lamellar structure with large amount of fine particles by using Cryo-SEM, suggesting that icariin was encapsulated in soymilk. These data supplied a novel strategy to improve the performance of icariin in functional foods.

Effect of high pressure homogenization on the interaction between corn starch and cyanidin-3-O-glucoside

The effects of high pressure homogenization (HPH) at different pressures (50, 100, 150 and 200 MPa) and temperatures (4, 20, 40, 60 and 80 °C) on the interaction between corn starch (CS) and cyanidin-3-O-glucoside (C3G) were investigated. Based on analyses of zeta potential, attenuated total reflection-flourier transformed infrared spectroscopy and binding rate after adding shielding agents, the main interaction force changed from electrostatic interaction to hydrogen bonds. In comparison, the interaction between CS and C3G exhibited greater strength at low temperatures and pressures. Especially, 4 °C/50 MPa HPH caused the most significant enhancement in binding rate and binding amount, from 9.56 % to 25.16 % and 0.96 μg/mg CS to 2.52 μg/mg CS, respectively. At this condition, the specific surface area of CS-C3G increased from 433.57 ± 0.91 m2/kg to 440.93 ± 1.01 m2/kg. Surface fluorescence reduction was observed by confocal laser scanning microscopy, further X-ray diffraction patterns indicated the retention of partial spatial structure. Therefore, HPH opened the entry channels, increased contact area and preserved steric hindrance, which increased hydrogen bonding sites. At high temperatures and high pressures (> 40 °C, > 100 MPa), the increasing free starch chains provided new hydrogen bonding sites. Overall, HPH was an effective method to enhance the interaction by affecting starch structure.

The Effect of High Pressure Homogenization on the Structure of Dual-Protein and Its Emulsion Functional Properties.

It has been proven that high-pressure homogenization (HPH) could improve the functional properties of proteins by modifying their structure. This study researched the effect of HPH on the structural and functional properties of whey-soy dual-protein (Soy Protein Isolation-Whey Protein Isolation, SPI-WPI). Different protein solution samples were treated with HPH at 30, 60, 90, 120 and 150 MPa, and the structure changed under different pressures was analyzed by measuring particle size, zeta potential, Fourier infrared spectrum (FTIR), fluorescence spectrum and scanning electron microscope (SEM). The results showed that HPH significantly reduced the particle size of SPI-WPI, changed the secondary and tertiary structures and improved the hydrophobic interaction between molecules. In addition, HPH significantly improved the solubility and emulsification of all proteins, and the improvement effect on SPI-WPI was significantly better than SPI and WPI. It was found that SPI-WPI treated with 60 MPa had the best physicochemical properties. Secondly, we researched the effect of HPH by 60 MPa on the emulsion properties of SPI-WPI. In this study, the SPI-WPI had the lowest surface tension compared to a single protein after HPH treatment. The emulsion droplet size was obviously decreased, and the elastic properties and physical stability of SPI-WPI emulsion were significantly enhanced. In conclusion, this study will provide a theoretical basis for the application of HPH in modifying the structure of dual-protein to improve its development and utilization in liquid specialty food.

Modifications to structural, techno-functional and rheological properties of sesame protein isolate by high pressure homogenization

In this study, we aimed to determine the effect of high pressure homogenization (HPH) at a pressure up to 150 MPa on microstructural, techno-functional and rheological properties of sesame protein isolate (SPI). HPH treatment caused a partial change in the secondary structure of SPI, however, the changes in surface hydrophobicity and free –SH groups, indicating HPH had significant effect on the tertiary structure. After the HPH treatment, the particles dispersed homogeneously with more rougher surface. Sesame proteins had the smallest particle size (0.79 μm) and highest zeta potential (38.83 mV) at 100 MPa pressure. The most developed water/oil holding capacity, emulsification and foaming properties were achieved at 100 MPa pressure. However, the maximum stable foam formation (83.33 %) was determined at 150 MPa pressure. When the shear rate is fixed as 50 1/s, an increase in the viscosity value of the samples treated with 100 and 150 MPa pressure was detected compared to the control sample, while the lowest viscosity was determined the ones treated at 50 MPa. In all samples except 50 MPa pressure-treated proteins, viscoelastic character became dominant with increasing frequency (G′ > G″). Modification with HPH resulted in a decrease of about 15 °C in the gelation temperature of SPI.

The Effects of High-Pressure Homogenization on Physicochemical and Functional Properties of Gelatin

The Effects of High-Pressure Homogenization on Physicochemical and Functional Properties of Gelatin

Effects of high-pressure homogenization on the physicochemical, foaming, and emulsifying properties of chickpea protein

In order to expand the utilization of chickpeas in various food products, this study investigated the effects of different homogenization pressures (0–150 MPa) and cycles (1–3) on the physicochemical, and functional properties of chickpea protein. After high-pressure homogenization (HPH) treatment, hydrophobic groups and sulfhydryl groups of chickpea protein was exposed which increased its surface hydrophobicity and decreased its total sulfhydryl content. SDS-PAGE analysis showed that the molecular weight of modified chickpea protein remained unchanged. The particle size and turbidity of chickpea protein significantly decreased with an increase in homogenization pressure and cycles. Furthermore, the solubility, foaming, and emulsifying properties of chickpea protein were all enhanced by HPH treatment. In addition, the emulsions prepared by modified chickpea protein showed better stability capacity due to its smaller particle size and higher zeta potential. Therefore, HPH might be an effective technique to improve the functional properties of chickpea protein.

High-pressure homogenization treatment of red seaweed Bangia fusco-purpurea affects the physicochemical, functional properties and enhances in vitro anti-glycation activity of its dietary fibers

In this study, high-pressure homogenization (HPH) technique was applied for the pretreatment of Bangia fusco-purpurea, and the effect of HPH on the composition, physiochemical and functional properties, and in vitro anti-glycation activity of dietary fiber from this seaweed (B. fusco-purpurea dietary fiber, BDF) was studied. Results showed that HPH significantly increased water-soluble dietary fiber (SDF) content in BDF. Water-holding capacity, oil-holding capacity, and glucose delay dialysis index of BDF were significantly enhanced after HPH treatment. Additionally, HPH significantly improved the in vitro anti-glycation activity of BDF by inhibiting the formation of advanced glycation end products (AGEs) and mitigating damage induced by AGEs on intestinal cells. These improvements could be attributed to the formation of the coarse and porous structure and greater exposure of hydroxyl groups of BDF caused by HPH treatment. These results implied the potential of HPH in seaweed processing and provided a scientific basis for the in-depth, comprehensive utilization of B. fusco-purpurea. Industrial relevanceHPH is an emerging non-thermal food processing technique with promising application potential in food industry. In this study, we found that HPH technique could significantly change the composition, improve physiochemical and functional properties and enhance anti-glycation activity of dietary fiber from seaweed B. fusco-purpurea. Our results validated the efficiency of HPH on dietary fiber modification, implying the potential of HPH in food industry and healthy industry.

The Impact of High-Pressure Homogenization and Thermal Processing on the Functional Properties of De-Fatted Chickpea Flour Dispersion

Defatted chickpea flour (DCF), a rich source of protein and starch, is frequently utilized in the food industry. Two crucial methods of modifying food materials are high-pressure homogenization (HPH) and heat treatment (HT). This study investigates the effect of co-treatment (HPH-HT) on the particle size, rheological behavior, and thermal characteristics of DCF suspensions. The results indicate that both HPH and HT can result in a more uniform distribution of particle size in the suspensions. The effect of HPH on G' was observed to be reductionary, whereas HT increased it. Nevertheless, the HPH-HT treatment further amplified G' (notably in high-concentration DCF), which demonstrates that the solid properties of DCF are improved. The apparent viscosity of the suspensions increased with individual and combined treatments, with the HPH-HT treatment of DCF12% exhibiting the most significant increase (from 0.005 to 9.5 Pa·s). The rheological behavior of DCF8% with HPH-HT treatment was found to be comparable to that of DCF12% treated only with HT. In conclusion, HPH-HT treatment shows a synergistic impact of HPH and HT on the rheological properties of DCF suspensions, however, it has limited effect on the particle size distribution and freeze-thaw stability.

Effect of High-pressure Homogenization on Structure and Properties of Soy Protein Isolate/polyphenol Complexes

Effect of High-pressure Homogenization on Structure and Properties of Soy Protein Isolate/polyphenol Complexes

Validation of High-Pressure Homogenization Process to Pasteurize Brazil Nut (Bertholletia excelsa) Beverages: Sensorial and Quality Characteristics during Cold Storage

The effect of high-pressure homogenization (HPH) on the inactivation of Escherichia coli and the stability of the quality properties of Brazil nut beverages were studied. E. coli was used as target microorganism to validate the HPH process (pressures from 50 to 180 MPa and inlet temperatures (Ti) from 25 to 75 °C). Cold storage (5 °C) for 21 days was conducted to establish the shelf-life of BN beverages, in terms of their microbiological, physical, physicochemical, and sensorial stability. HPH-treated samples were compared to pasteurized BN beverages (63 °C for 20 min). The combination of Ti and the pressure of the HPH process (50 to 150 MPa/75 °C and 180 MPa/25 °C) had a significant effect on E. coli inactivation (8.2 log CFU/mL). During storage at 5 °C, the growth of mesophilic aerobes in processed BN beverages was controlled by the HPH process. Oxidative stability (TBAR assay) and physicochemical properties (pH, acidity, and °Brix) were evaluated during cold storage, showing good stability. Additionally, HPH-treated beverages showed a reduction in their particle size and the formation of more stable protein aggregates, which favored the beverages’ whiteness (color). The HPH process could be an alternative to pasteurization to obtain Brazil nut beverages with an acceptable microbiological shelf life (≥21 days at 5 °C) and high-quality characteristics without the use of any additives.

Effect of high-pressure homogenization on Ca2+ -induced gel formation of soybean 11 S globulin.

High-pressure homogenization (HPH) is commonly used as a non-thermal processing technique for soybean and soy protein products, and the preparation of soy protein gel products often requires the synergistic effect of HPH and heat treatment. The dissociative association behavior of 11 S is the key to the protein gel formation state. In this study, therefore, 11 S thermal gels were prepared by high-pressure homogenization and co-induction (90 °C, 30 min) (adding Ca2+ to promote gel formation before heat treatment), and the effects of different high-pressure homogenization pressures (0-100 MPa) and co-treatment on the dissociative association behavior of 11 S protein, gel properties, and microstructure of 11 S gels were investigated. The results showed that HPH at higher pressures led to the breaking of disulfide bonds of aggregates and disrupted non-covalent interactions in protein aggregates, leading to collisions between protein aggregates and the reduction of large protein aggregates. High-pressure homogenization treatment at 60 MPa improved the gel properties of 11 S more. The HPH combined with heating changed the binary and tertiary structure of 11 S soy globulin and enhanced the hydrophobic interaction between 11 S molecules, thus improving the gel properties of 11 S. The change in intermolecular forces reflected the positive effect of HPH treatment on the formation of denser and more homogeneous protein gels. In conclusion, high-pressure homogenization combined with heating can improve the properties of 11 S gels by changing the structure of 11 S protein, providing data and theoretical support for soy protein processing and its further applications. © 2022 Society of Chemical Industry.

High pressure homogenization to boost the technological functionality of native pea proteins

Pea proteins are being increasingly used for the formulation of plant-based products, but their globular structure and the presence of aggregates can affect their technological properties. In this study, the effect of high pressure homogenization (HPH) at different intensities (60 and 100 MPa) was investigated as a pre-treatment to modulate the techno-functional properties of a pea protein isolate (IP) extracted through an alkaline extraction/isoelectric precipitation process. SDS-PAGE, circular dichroism, thermal properties, total free sulfhydryl groups, antioxidant capacity and reducing properties were evaluated along with technological indices as solubility, WHC and OHC, interfacial tension and emulsifying capacity. HPH treatments were able to unfold and modify proteins structure, leading also to a change of the relative abundance of pea protein globulins (SDS-PAGE) and of the vicilin to legumin ratio. Solubility, WHC and OHC were improved, while interfacial tension and emulsifying capacity were weakly affected. However, an enhanced physical stability over time of the emulsions prepared with the 60 MPa-treated protein was found, likely as an effect of the decreased ratio between vicilin and legumin after treatment.Results of this study will contribute to deepen the effect of the HPH technology used as pre-treatment, adding useful results and expanding knowledge about the structure and techno-functional properties of native and modified pea proteins.