Pectin Complexes Research Articles

Sustainable polyelectrolyte complexes of pectin and chitosan as adsorbents for heavy metal ions from surface water

Sustainable polyelectrolyte complexes of pectin and chitosan as adsorbents for heavy metal ions from surface water

The Influence of pH on the Emulsification Properties of Heated Whey Protein-Pectin Complexes.

Interactions between proteins and polysaccharides could improve protein functional properties. Most studies focus on the formation of complex coacervates at pHs < pI. Much less attention has been given to the interactions at pHs > pI, especially when the mixtures are heated. The objective of this study was to investigate the emulsification properties of heated whey protein isolate (WPI) and pectin complexes formed at near neutral pHs. Heated soluble complexes (Cpxs) were formed by heating mixed WPI (3 wt% protein) and pectin (0 to 0.60 wt%) at pH 6.0, 6.5, or 7.0 at 85 °C for 30 min. Emulsions (5 wt% oil, 0.5 wt% protein, and pH 5.5) were characterized by measuring droplet size, zeta potential, rheological properties, and creaming stability. The results showed that, regardless of heating pH, Cpxs formed more stable emulsions with significantly smaller droplet sizes, higher negative charges, and less shear-thinning behavior in comparison to emulsions stabilized by heated WPI (p < 0.05). At fixed pectin concentrations, the emulsions stabilized by Cpx formed at pH 7.0 were the most stable. Increasing pectin concentrations led to a decrease in mean droplet sizes and an increase in negative charge. Maximum stability was achieved with the emulsion stabilized by Cpx formed with 0.60 wt% pectin at pH 7.0. The formation of Cpxs under proper conditions will allow for the utilization of WPI in a wider range of applications and fulfill the consumer need for clean label food products.

Fabrication and Characterization of Docosahexaenoic Acid Algal Oil Pickering Emulsions Stabilized Using the Whey Protein Isolate-High-Methoxyl Pectin Complex.

In this study, the whey protein isolate-high-methoxyl pectin (WPI-HMP) complex prepared by electrostatic interaction was utilized as an emulsifier in the preparation of docosahexaenoic acid (DHA) algal oils in order to improve their physicochemical properties and oxidation stability. The results showed that the emulsions stabilized using the WPI-HMP complex across varying oil-phase volume fractions (30-70%) exhibited consistent particle size and enhanced stability compared to emulsions stabilized solely using WPI or HMP at different ionic concentrations and heating temperatures. Furthermore, DHA algal oil emulsions stabilized using the WPI-HMP complex also showed superior storage stability, as they exhibited no discernible emulsification or oil droplet overflow and the particle size variation remained relatively minor throughout the storage at 25 °C for 30 days. The accelerated oxidation of the emulsions was assessed by measuring the rate of DHA loss, lipid hydroperoxide levels, and malondialdehyde levels. Emulsions stabilized using the WPI-HMP complex exhibited a lower rate of DHA loss and reduced levels of lipid hydroperoxides and malondialdehyde. This indicated that WPI-HMP-stabilized Pickering emulsions exhibit a greater rate of DHA retention. The excellent stability of these emulsions could prove valuable in food processing for DHA nutritional enhancement.

Effects of different solid particle sizes on oat protein isolate and pectin particle-stabilized Pickering emulsions and their use as delivery systems

Oat protein isolate (OPI)/high methoxyl pectin (HMP) complexes (OPP) were prepared to stabilized Pickering emulsions and applied as nutraceutical delivery systems. The different mass ratios and pH changed the interactions between OPI and HMP that caused the different size of OPP. Specifically, smaller particle size of OPP (125.7–297.6 nm) were formed when hydrophobic interactions along with electrostatic forces predominant in OPP (OPI:HMP = 3:1, pH 4, 5). Among these particles, OPP-2 could stabilize Pickering emulsion efficiently through formation of dense interfacial film, which exhibited the highest apparent viscosity and the smallest average droplet size (23.39 μm). Moreover, OPP-2 stabilized Pickering emulsions with superior stability not only exhibited higher encapsulation efficiency of 85.63%, but also could control curcumin release in simulated gastrointestinal fluids to improve curcumin's bioaccessibility. These results verified the possibility of OPP to be a Pickering emulsions stabilizer, and also identified its potential to be a stable delivery system for bioactive compounds.

Rheological Properties and Swelling Kinetics of Hydrogels Based on Polymer Complexes of Pectin and Arabinogalactan

Rheological Properties and Swelling Kinetics of Hydrogels Based on Polymer Complexes of Pectin and Arabinogalactan

Effect and mechanism of pectin for modulating bitter taste of soyasaponin

Soyasaponins (Ssa) have various biological benefits for the human body. However, they are one of the main factors contributing to the bitter taste of certain soybean-based foods. In this study, the case interaction between pectin and Ssa was investigated by us, as well as the impact of pectin addition on the bitter taste of Ssa. The findings revealed that the thermal stability of Ssa–pectin complexes was higher than that of Ssa–mucin complexes. Fluorescence spectroscopy and isothermal titration calorimetry revealed that pectin interferes with the binding of Ssa to mucin by interacting with Ssa, thereby disrupting the Ssa binding process. As the proportion of pectin increases, the comprehensive score also increases. This confirms that pectin can effectively reduce the bitterness and astringency of Ssa, signifying its importance in further exploration of the mechanism by which Ssa–pectin complexes influence the presentation of bitterness.

Application of complexes from phycocyanin and pectin in a model beverage system

The blue-appearing phycocyanin from the cyanobacteria Arthrospira platensis undergoes severe color losses during food production or storage. Thus, many studies have looked at stabilizing phycocyanin against processing conditions such as heat with biopolymer complexes. The promising results have not yet been applied to beverage systems. In this study, complexes of pectin and phycocyanin were evaluated for color stability in double distilled water and a model beverage system. The color stability was tested under severe storage conditions. With a z-average diameter of 326 ± 26 nm, the complexes of phycocyanin and pectin remained smaller than pure phycocyanin (415 ± 71 nm) after heating and storage for 13 days. This could assure a better colloidal stability of the color. Kinetic modelling showed that the color degradation was slowed down by the application of complexes between phycocyanin and pectin from a half-life (t1/2) of 74 days to 117 days. A decreased color degradation could be confirmed in the model beverage although an initial color shift which needs to be considered. The color difference between the original hue at day 0 and the samples stained with phycocyanin alone exceeded that of the beverages stained with the complexes from day 10 to 13.

Interactions of Native Maize Starch Components with Pectin Using Extrusion

AbstractNative starch exhibits undesirable properties in the final product when used as an additive. Recently, the effects of the interaction between starch and hydrocolloids on the techno‐functional properties of starch have been studied. However, this interaction has not yet been applied to a real food system. Therefore, in this work, the techno‐functional properties of starch–pectin complexes formed by extrusion are investigated. Mixtures of isolated native Pozolero maize starch “HPZ1” and pectin of low degree of methyl‐esterification at four concentrations (0%, 2%, 5%, and 7%) are used. The starch–pectin blends are processed in a single screw extruder with constant variables: temperature, screw speed, and moisture. Morphology, X‐ray diffraction, thermal properties, and techno‐properties are studied. A protective effect of pectin on the starch granules is observed, as evidenced by a matrix involving starch granules. Extrusion results in a partial gelatinization of the starch granules and alters their thermal and pasting properties with the peak temperature increasing with increasing pectin concentration. Extrusion allows both carbohydrates to interact with each other. Finally, the results show that the starch–pectin complexes are ingredients with desirable techno‐functional properties that can be integrated into a food system and add value to Mexican criollo maize.

Microencapsulation of vitamin E by gelatin-high/low methoxy pectin complex coacervates: Effect of pH, pectin type, and protein/polysaccharide ratio

In this study, gelatin (GA), high-methoxyl pectin (HMP) or low-methoxyl pectin (LMP) were used to prepare complex coacervates, and effect of pectin type, pH, and gelatin-pectin ratio on formation and physiochemical properties of complex coacervates were deeply investigated. Furthermore, vitamin E (VE) was encapsulated using GA-HMP/LMP complex coacervates. The GA-HMP/LMP complex coacervates and GA-HMP/LMP-VE microcapsules were optimized and characterized. At the gelatin-pectin ratios of 2:1 and 3:1 and pH of 4.0, the GA-HMP and GA-LMP had the maximum yield of 54.67 ± 1.82% and 59.33 ± 1.49%, and turbidity of 1.33 ± 0.02 and 1.30 ± 0.04, respectively, and GA-HMP/LMP were close to zero potential at this point, indicating that the strength of electrostatic interaction was strongest. The GA-LMP and GA-HMP displayed spherical and irregular short-rod like appearance, respectively, and more aggregates and denser network were formed at gelatin-pectin ratio of 3:1, especially in GA-HMP3:1. The formation of GA-HMP/LMP complex coacervates was driven by electrostatic interaction, and GA-HMP3:1 had the optimum thermal stability. Except GA-HMP2:1-VE, the prepared and optimized VE mirocapsules by GA-LMP and GA-LMP complex coacervates showed spherical state and uniform particle size. The GA-HMP2:1-VE and GA-HMP3:1-VE possess the highest hygroscopicity and wettability of 109.08 ± 7.66 s and 26.67 ± 0.85 g/100g, respectively. The GA-HMP3:1-VE microcapsules had the highest encapsulation efficiency of 82.67 ± 1.77 %. Results of differential scanning calorimetry and release behavior in hot-water indicated that the microcapsules had excellent thermal stability. Furthermore, the GA-HMP and GA-LMP made VE stable in gastric stages and sustainable release in intestinal stages.

Pectin-coated whey protein isolate/zein self-aggregated nanoparticles as curcumin delivery vehicles: Effects of heating, pH, and adding sequence

In this work, pectin was employed as a coating material to fabricate zein/whey protein isolate (WPI)/pectin complex nanoparticles via a pH-adjusted and heat-induced electrostatic adsorption process for potential oral administration applications of curcumin. Factors such as the order of raw material addition, heating temperature and pH, and zein concentration were comprehensively examined. In addition to electrostatic interactions, Fourier transform infrared and fluorescence spectroscopy indicated that hydrophobic interactions and hydrogen bonds were also involved in the development of complex nanoparticles. The complex nanoparticles obtained not only improved the antioxidant activity of curcumin in aqueous phase, but also contributed to its controlled release under gastrointestinal conditions. Our findings revealed that the heating pH and adding sequence of raw materials had a notable impact on the properties of complex nanoparticles, and that pectin coating had an exceptional stabilizing effect on complex nanoparticles under gastrointestinal circumstances. This study provides novel insights and perspectives for the preparation of polysaccharide-protein complex nanoparticles, signifying the potential use of zein/WPI/pectin complex nanoparticles as delivery vehicles in the functional food and pharmaceutical industries.

Interaction mechanisms of peanut protein isolate and high methoxyl pectin with ultrasound treatment: The effect of ultrasound parameters, biopolymer ratio, and pH.

Ultrasound could effectively change molecular structure of proteins, polysaccharides, and their interactions, and was used to treat the peanut protein isolate-high methoxy pectin (PPI-HMP) complexes in this study. Effects of different ultrasound parameters, PPI-HMP mixing ratio (40:1-5:2), and pH (2.0-8.0) on the PPI-HMP interactions were investigated. Turbidity, solution appearance, and Zeta-potential analysis revealed an electrostatic interaction between PPI and HMP from pH 2.0 to pH 6.0. Ultrasound changed the tertiary structure conformation of PPI according to the surface hydrophobicity analysis. Increased ultrasound power density and pH broke the hydrogen bonds between the complexes according to Fourier transform infrared spectroscopy analysis. Apparent viscosity and confocal laser scanning microscopy analysis showed that appropriate ultrasound treatment (5.43W/cm3, 25min, 25°C) reduced the viscosity of the complexes, and enhanced the electrostatic and hydrophobic interactions between PPI and HMP. These findings will contribute to the application of PPI-HMP complexes in the food industry.

Fabrication of Whey Protein Isolate-Pectin Nanoparticles by Thermal Treatment: Effect of Dynamic High-Pressure Treatment.

This study investigated the impact of dynamic high-pressure (DHP) treatment on the ability of whey protein isolate (WPI) to form associative complexes with pectin and to form aggregate particles after their subsequent heat treatment. Light scattering showed that DHP treatments disrupted preexisting WPI aggregates and assembled pectin chains. Complexes formed from WPI/pectin mixtures at pH 4.5 were an order of magnitude smaller when formed after DHP treatment, regardless of the degree of esterification. WPI/pectin complexes formed after DHP treatment were more stable against subsequent pH neutralization than complexes formed without DHP treatment, and WPI/high-methoxyl pectin (HMP) complexes had greater stability than WPI/low-methoxyl pectin (LMP) complexes. WPI/pectin particles prepared by thermal treatment of complexes at pH 4.5 were also smaller when prepared after DHP treatment. WPI/HMP particles were stable to subsequent pH neutralization, while WPI/LMP particles became larger after neutralization.

Juice yield and pectin indicators in apple and carrot pomace

Background: Pectin exhibits different properties based on its degree of esterification, forming gels and serving as a structure-forming agent in food products, or forming complexes with heavy metal ions, finding applications in the development of therapeutic products for the elimination of heavy metal ions from the human body. Context and purpose of this study: The purpose of this study is to investigate the influence of enzymatic treatment on the yield and quality of apple and carrot juices, as well as the quality parameters of pectin in pomace. Our objectives were to select an enzymatic preparation for processing apple and carrot pomace and to study changes in the properties of pectins present in the pomace depending on the dosage of the enzyme preparation.Results: The results of our experiments revealed that for apple pomace processing, it is more beneficial to use the enzyme preparation Vegazym M with a dosage of 0.09% of the pomace mass, while for carrot pomace processing, the enzyme preparation Fructozym MA with a dosage of 0.07% of the pomace mass proved to be the most suitable. These enzyme preparations in the specified amounts ensure maximum juice yield. It has been established that changing the dose of enzymes changes the complexing properties of pectin, which allows its use in food products with therapeutic and prophylactic properties.Conclusions: The enzyme preparations allow for specific modifications, such as pectin modification in this case, enabling the versatile use of pectin as either a structure-forming agent or for the development of therapeutic and preventive food products.Keywords:Apple and carrot juices, enzyme preparations, apple and carrot pomace, pectin, soluble and insoluble pectin, degree of esterification and pectin complexation, functional products.

Effect of pH on the formation mechanisms, emulsifying properties and curcumin encapsulation of oat protein isolate–high methoxy pectin complexes

Oat protein isolate (OPI) has high nutritional value but poor emulsifying properties. The purpose of modifying the OPI with high methoxyl pectin (HMP) was to improve emulsification. In this work, an oat protein isolate (OPI)–high methoxyl pectin (HMP) complex was constructed by changing the pH, and the interactions, formation mechanism and potential use of the OPI–HMP complex as a food emulsifier were explored. The presence of HMP caused structural changes in the OPI, and the changes were pH dependent. When the OPI to HMP mass ratio was 3:1, the critical pH for the phase behavior of OPI–HMP was 5.0. When the pH was greater than 5.0, the OPI and HMP were codissolved in the composite system mainly through electrostatic repulsion. When the pH was 5.0, a soluble OPI–HMP complex was formed by a combination of electrostatic attractions, hydrophobic interactions and hydrogen bonding. At pH values below 5.0, other aggregates of HMP and OPI were generated through electrostatic attraction and hydrogen bonding and formed insoluble aggregates. When the OPI to HMP mass ratio was 3:1 and the pH was 5.0, the particle sizes of the emulsion were the smallest at 8.75 μm due to the strong electrostatic interactions. The emulsification activity and stability were much higher than those of the OPI, and they formed dense osmotic networks, which protected the curcumin. The rates for curcumin encapsulation and retention reached 83.87 ± 1.50% and 88.70 ± 2.50%, respectively, and the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging rate was maintained at a high level (approximately 72%). These results confirmed the possibility of using the OPI-HMP complex emulsions as excellent and stable nutraceutical delivery systems for lipid soluble bioactive compounds in food and biomedical applications.

INTERACTION OF PECTIN WITH THE ANTIBACTERIAL DRUG NITROXOLINE

The process of macromolecular complexation of natural polymer pectin with nitroxoline, which has antibacterial activity, was studied in order to increase the solubility of the drug and, consequently, its therapeutic efficiency. By potentiometric titration it has been shown that in dilute aqueous solutions in a wide range of slightly acidic, neutral, and alkaline pH medium, the electrostatic binding of nitroxoline with pectin occurs. In the most optimal for medical preparations neutral region pH 7 the conversion depth of this reaction was calculated. The depth of conversion of pectin carboxyl groups ɵ1 for various studied ratios P : NOC=10 : 1, 5 : 1, 3 : 1 is 0.052, 0.076, and 0.095, respectively. The corresponding values of the conversion depth for nitroxoline ɵ2 are somewhat larger and amount to 0.52, 0.38, 0.32, respectively, for the studied ratios. That is, the calculation shows that not all reactive carboxyl groups of pectin and amino groups of the medicinal substance participate in electrostatic interaction.&#x0D; By the viscometry method it has been established the decrease of the pectin solution viscosity in the presence of nitroxoline. This indicates that electrostatic bonding of the low molecular weight medicinal substance NOC leads to the hydrophobization of the pectin macromolecule.&#x0D; Comparative data, obtained by the method of derivatographic analysis, indicate, that the thermal characteristics of the studied complex of nitroxoline with pectin differ from the thermal parameters of the initial components and is thermally more stable. This confirms the formation of the product of chemical interaction - the complex of pectin with NOC.

Correlationship between self-assembly behavior and emulsion stabilization of pea protein-high methoxyl pectin complexes treated with ultrasound at pH 2.0

This study investigated the effects of ultrasound on the self-assembly behavior of pea protein (PP)-high methoxyl pectin (HMP) complexes at pH 2.0 through transmission electron microscopy (TEM), Fourier transform infrared spectroscopy (FTIR), and intrinsic fluorescence analysis. The emulsion stabilization mechanism of PP-HMP treated with ultrasound (PP-HMP-US) was also elucidated. The results indicated that ultrasound increased the emulsifying activity index (EAI) and emulsifying stability index (ESI) of PP-HMP. Moreover, PP-HMP-US-based emulsions formed small, dispersed oil drops, which were stable during storage. PP-HMP- and PP-HMP-US-based emulsions did not demonstrate any creaming. The TEM results revealed that ultrasound can regulate the self-assembly behavior of PP and HMP to form spherical particles with a core–shell structure. This structure possessed low turbidity, a small particle size, and high absolute zeta potential values. The FTIR and intrinsic fluorescence spectra demonstrated that ultrasound increased the α-helix and β-sheet contents and exposed the tryptophan groups to more hydrophilic environments. Ultrasound also promoted the PP-HMP self-assembly through electrostatic interaction and improved its oil–water interfacial behavior, as indicated by the EAI and ESI values of PP-HMP-US-based emulsions. The current results provide a reference for the development of an innovative emulsifier prepared by ultrasound-treated protein–pectin complexes at low pH.

Complex Modification Orders Alleviate the Gelling Weakening Behavior of High Microbial Transglutaminase (MTGase)-Catalyzed Fish Gelatin: Gelling and Structural Analysis.

In this paper, the effects of different modification orders of microbial transglutaminase (MTGase) and contents of pectin (0.1-0.5%, w/v) on the gelling and structural properties of fish gelatin (FG) and the modification mechanism were studied. The results showed that the addition of pectin could overcome the phenomenon of high-MTGase-induced lower gelling strength of gelatin gels. At a low pectin content, the modification sequences had non-significant influence on the gelling properties of modified FG, but at a higher pectin content (0.5%, w/v), P0.5%-FG-TG had higher gel strength (751.99 ± 10.9 g) and hardness (14.91 ± 0.33 N) values than those of TG-FG-P0.5% (687.67 ± 20.98 g, 12.18 ± 0.45 N). Rheology analysis showed that the addition of pectin normally improved the gelation points and melting points of FG. The structural results showed that the fluorescence intensity of FG was decreased with the increase in pectin concentration. Fourier transform infrared spectroscopy analysis indicated that the MTGase and pectin complex modifications could influence the secondary structure of FG, but the influenced mechanisms were different. FG was firstly modified by MTGase, and then pectin (P-FG-TG) had the higher gelling and stability properties.

Structural correlations of complexation of apple pectin with imidazole and L-histidine methyl ester

The thermodynamic and structural study of the complex formation of apple pectin with structural analogs of histidine (imidazole and its methyl ester) was carried out using spectral methods. The composition, stability constants of the complexes, and standard thermodynamic characteristics (Δ G° , Δ H° , Δ S° ) of the complex formation process were determined. The decisive contribution of the imidazole fragment of the amino acid to the stability of the pectin-histidine complex is shown. The esterification of the carboxyl group of histidine, its conversion into methyl ester, has an insignificant effect on the efficiency of complex formation with pectin, leading only to a slight increase in binding.

Effects of multi-frequency ultrasound on sodium caseinate/pectin complex: Emulsifying properties, interaction force, structure and correlation

This study aimed to improve the emulsification properties of the sodium caseinate (Cas) and pectin (Pec) complex using multi-frequency power ultrasound to regulate the complexation of Cas and Pec. The results revealed that optimal ultrasonic treatment (Frequency 60 kHz, power density 50 W/L, and time 25 min) led to a 33.12 % increase in emulsifying activity (EAI) and a 7.27 % increase in emulsifying stability index (ESI) of the Cas-Pec complex. Our results demonstrated that electrostatic interactions and hydrogen bonds were the main driving forces for complex formation, and these were reinforced by ultrasound treatment. Moreover, it was observed that ultrasonic treatment improved the surface hydrophobicity, thermal stability, and secondary structure of the complex. Scanning electron microscopy and atomic force microscopy analyses revealed that the ultrasonically prepared Cas-Pec complex had a dense, uniform spherical structure with reduced surface roughness. It was further confirmed that the complex's emulsification properties were highly correlated with its physicochemical and structural properties. Multi-frequency ultrasound changes the interaction by regulating protein structure and ultimately acting on the interfacial adsorption behavior of the complex. This work contributes to expanding the role of multi-frequency ultrasound in modifying the emulsification properties of the complex.

Structural Features of the Apple Pectin Complex Formation with Imidazole and L-Histidine Methyl Ester

Structural Features of the Apple Pectin Complex Formation with Imidazole and L-Histidine Methyl Ester