Pectin Complexes Research Articles

Protein-polysaccharide complex coated W/O/W emulsion as secondary microcapsule for hydrophilic arbutin and hydrophobic coumaric acid

This study aimed to examine the modification effect of whey protein concentrate (WPC), WPC-gum arabic (WPC-GA) or WPC-high methoxyl pectin (WPC-PEC) complex to tailor-modify W/O/W emulsion for secondary microencapsulation of hydrophilic arbutin and hydrophobic coumaric acid. The stability and rheological properties of coated emulsions, encapsulation yield, release and degradation kinetics of arbutin and coumaric acid were investigated. Results revealed that WPC-PEC complex (at the ratio of 1:3) coating W/O/W emulsion exhibited the highest viscosity and stability, with the highest encapsulation yield of 91.08% for arbutin and 80.92% for coumaric acid, respectively. Tighter coating structure of the WPC-PEC complex (1:3) forming a stronger gel network structure was confirmed, accounting for the larger mean particle size of 569.67 nm. Moreover, the WPC-PEC (1:3) coating W/O/W emulsion also showed controlled release of arbutin and coumaric acid in simulated conditions. The k value of degradation kinetics for arbutin (7.99 × 10−4 at pH = 1.2, 4.19 × 10−4 at 90 °C and 7.52 × 10−4 at UV-C treatment) and coumaric acid (5.18 × 10−4 at pH = 1.2, 3.24 × 10−4 at 90 °C and 6.90 × 10−4 at UV-C treatment) indicated low degradation rate. The present study revealed that the WPC-PEC (1:3) coating W/O/W emulsion could provide a better synergistic effect on higher encapsulation yield and stability of arbutin and coumaric acid.

A facile water-induced complexation of lycopene and pectin from pink guava byproduct: Extraction, characterization and kinetic studies

The redfleshed pulp discarded from pink guava puree industry is a rich source of lycopene and pectin. In this study, we developed a facile extraction process employing water as the primary extraction medium to isolate the lycopene and pectin from pink guava decanter. When the decanter was suspended in water, the complexation of lycopene and pectin formed the cloudy solution, where the colloidal complexes were recovered through centrifugation. The presence of lycopene and pectin in the complex was confirmed by the spectroscopic, microscopic and chromatographic analyses. The lycopene fractionated from the complexes had a purity level of 99% and was in all-trans configuration. The colloidal complexes yielding the highest concentration of lycopene was obtained at pH 7, 1% (w/v) solid loading and 25 °C. The experimental data of time-course extraction of lycopene-pectin complex were best fitted with two-site kinetic model, hinting the fast- and slow-release phases in the extraction process.

Enzyme-responsive mechanism based on multi-walled carbon nanotubes and pectin complex tablets for oral colon-specific drug delivery system

The purpose of this work was to explore the potential application of MCNT as a colon-specific delivery system based on the enzyme responsive mechanism. A novel type of enzyme-sensitive colon-specific tablet (PM-tablet) based on pectin and multi-walled carbon nanotube (MCNT) was prepared by wet granulation tabletting method. The PM-tablet in the presence of pectinase exhibited enzyme degradation release and achieve a precise release in the colon. Our study had proposed a novel idea for the application of MCNT on the oral colon-specific drug delivery system.

Protection of native lactoferrin under gastric conditions through complexation with pectin and chitosan

The aim of this work was to encapsulate native bioactive lactoferrin (Lf) in pectin-based colloidal delivery systems with and without a chitosan (CS) coating, and to explore their fate under digestive conditions. We compared the abilities of low methoxyl (LM) pectin and high methoxyl (HM) pectin to form complexes with Lf at different mass ratios. LM pectin led to a smaller particle size (256 nm) and a higher Lf encapsulation efficiency (>72%) than HM pectin because of its greater negative charge (−43.6 versus −16.4 mV). After validating the retention of the bioactivity of native Lf (antimicrobial activity) in these complexes, we coated the Lf‒LM pectin complex with a layer of CS, which had no significant effect on the Lf encapsulation but improved the colloidal stability under gastric conditions. Both Lf‒pectin complexes and chitosanCS-coated complexes retained >90% of the Lf from release in simulated gastric fluid. This resulted in gastric protection of Lf against pepsin-mediated hydrolysis for at least 60 min, relative to free Lf solution. CS-coated complexes also delayed the degradation of released Lf, possibly because of the interaction between this cationic biopolymer and pepsin.

Synthesis and physicochemical properties of the pectin complexes with Xymedon

The formation of stable complexes of pectin polysaccharides with 1-(2-hydroxyethyl)-4,6- dimethyl-1,2-dihydropyrimidin-2-one (Xymedon drug) was shown by UV and IR spectro scopy, dynamic light scattering, and polarimetry. The stoichiometry of the complexes was determined, and their synthesis conditions were optimized. Specific features of the thermal decomposition of pectin and synthesized complexes with Xymedon were studied by the TG/DSC method. The results obtained allow one to substantially extend ranges of using Xymedon in medicine.

Application of Transglutaminase Crosslinked Whey Protein–Pectin Coating Improves Egg Quality and Minimizes the Breakage and Porosity of Eggshells

It is well known that an effective way to improve the quality attributes of food is the use of coatings. Moreover, there is evidence of the use of dairy byproducts to design coatings to improve the shelf life of food products. This study was conducted to explore the effectiveness of a film forming solution containing whey protein–pectin complex enzymatically reticulated by transglutaminase (TGase) applied as a coating on eggshells to preserve the internal quality of eggs stored under environmental conditions (25 ± 1 °C and 35% HR) during 15 days storage. Eggs properties tested included yolk index, albumen and yolk pH, albumen CO2 content, water loss, shell strength, and microbial permeability through the shell. The results showed that the coating maintained a higher yolk index and albumen carbon dioxide content, reduced the weight loss and increased both albumen and yolk pH values with respect to the uncoated eggs. All coated eggshells showed greater strength than those of uncoated eggs. Moreover, by using Blue Lake dye penetration method we demonstrated that the coating reduced the Blue Lake dye penetration confirming the effectiveness of the coating on the reduction of post-wash bacterial penetration. These results suggest that the studied coating can be useful to preserve internal egg quality but also to reduce the breakage of eggshell and egg microbial contamination. Based on this result we can conclude that the coating made with whey protein–pectin crosslinked by TGase could be an effective strategy to increase the shelf life of eggs preserved in environmental conditions and to reduce economic losses due to the eggs breakage during their marketing.

Pectin from Black Tomato Pomace: Characterization, Interaction with Gallotannin, and Emulsifying Stability Properties

Hydrochloric acid and ammonium oxalate are used to refine pectin from black tomato pomace. The characterization of pectin‐yield, galacturonic acid (GalA) content, degree of methoxylation, neutral sugar composition and molecular weight, interaction with gallotannin as well as emulsion stability are investigated. Hydrochloric acid‐extracted pectin (HEP) and chelating agent‐extracted pectin (ChEP) satisfy the commercial pectin requirements (GalA% > 65%) and are smooth pectin with high homogalacturonan segments (70.6 and 65.4%, respectively). As the structure results suggest, HEP has fewer and shorter branches compared with ChEP. As titration results suggest, gallotannin is bound by pectin and forms insoluble gallotannin–pectin complexes, the maximum combination gallotannin to pectin mass ratios are 0.28 and 0.47 for HEP and ChEP, respectively. Yet as distribution of volume‐weighted diameter, micrographs and values of surface‐weighted diameter suggest, the emulsions stabilized by HEP show better stability than ChEP. The study shows that ChEP is a better additive in beverages containing gallotannin, while HEP has better emulsifying stability.

Influence of low methoxyl pectin on the physicochemical properties of sodium caseinate‐stabilized emulsions

AbstractTwo strategies of emulsion preparation, stabilization by sodium caseinate (CAS)/low methoxyl pectin (LMP) complexes formed in advance, and stabilization by the layer‐by‐layer (LBL) method, were compared. In aqueous solution, at a constant CAS concentration (5 g/L), the gradual addition of LMP resulted in an increase in turbidity of the solution caused by the increasing formation of insoluble complexes. The zeta potential change showed that the interactions are mainly due to an electrostatic mechanism. The spectrofluorometric studies as well as the spectroscopic analysis in the UV–visible region have shown that the interactions with LMP caused a change in the secondary and tertiary structures of the protein. Then, these complexes were used for stabilizing oil/water emulsions. The emulsions stabilized by complexes formed in advance and LBL method were characterized by measuring zeta potential, dynamic viscosity, serum index, and particle size distribution. The results showed that, at low LMP concentrations, complexes‐stabilized emulsions were more stable than LBL‐stabilized ones, while at high LMP concentrations, LBL‐stabilized emulsions showed better stability.Practical applicationsThese results would be useful during the development of encapsulation systems having hybrid interfaces in order to better control the release of hydrophobic active molecules like essential oils. These molecules have various benefits like antioxidant and antimicrobial activities, which could be exploited for food biopreservation. One of the major problems for application in food preservation of these active molecules is their great sensitivity to the environmental stress (temperature, pH…), their low water‐solubility, their interactions with food components, and their pronounced odor and flavor. The encapsulation of these molecules in the developed emulsions containing the proper concentration of LMP could be a suitable solution to protect and release these lipophilic molecules in foods.

Gelatin and pectin complex coacervates as carriers for cinnamaldehyde: Effect of pectin esterification degree on coacervate formation, and enhanced thermal stability

This study developed the multinuclear microcapsules by the complex coacervation between gelatin (G) and high methyl pectin (HMP), low methyl pectin (LMP) as a delivery system for cinnamaldehyde. The parameters affecting the formation of such carriers were investigated by dynamic light scattering and microscopic techniques. Fluorescence analysis and Fourier-transform infrared (FTIR) were used to study protein conformation change during coacervate formation between gelatin and pectin. The results showed that high yield of coacervates with good size and morphology occurred at pH 4.23 and 4.37 for G/HMP with a ratio of 3:1 and G/LMP with a ratio of 6:1 respectively. Fluorescence and FTIR analysis further confirmed their electrostatic interaction and gelatin molecules exhibited a conformational change following the complexation. Thermal gravimetric analysis revealed that microencapsulation of cinnamaldehyde by complex coacervation using gelatin and pectin significantly increased the degradation temperature from 180-220 °C to 350–400 °C. Moreover, high methyl pectin revealed a higher encapsulation efficiency (89.2%) and controlled release of cinnamaldehyde in hot water (33% for 120 min at 80 °C). It could be suggested conformation of pectin types and gelatin might significantly contribute to the overall complexation and cinnamaldehyde microcapsule properties. These findings could be useful for design an ideal carrier to deliver flavors like cinnamaldehyde by complex coacervation using protein and different pectin types.

Insignificance of lactose impurities on generation and structural characteristics of thermally stabilised whey protein-pectin complexes

We studied the impact of lactose impurities (0, 130, 150 mm) on micro- and macro-structural characteristics of thermally stabilised whey protein–pectin complexes (WPPC) by varying biopolymer concentration [chigh = 5.0% whey protein isolate (WPI) + 1.0% pectin; cmed = 2.75% WPI + 0.55% pectin; clow = 0.5% WPI + 0.1% pectin], shear rate (0, 150, 500 s−1) and scale (lab/pilot plant). We demonstrated that ≤150 mm lactose had no significant effect on the microstructure of WPPC, as investigated by fluorescence spectroscopy and browning measurements. Unfolding of β-lactoglobulin within WPPC depended on the biopolymer concentration, being strongest at chigh. Measured browning was attributed to reactions between whey proteins and neutral sugars in pectin side chains. Particle size was unaffected by lactose, but showed an increase with biopolymer concentration and a decrease with shear rate. Thus, WPPC can likely be generated using whey powders with lactose impurities or other protein sources of lower purity.

Effects of amidated low methoxyl pectin on physiochemical and structural properties of polymerized whey proteins

ABSTRACTThis study aimed to investigate effects of amidated low methoxyl (ALM, 0.3%, w/v) pectin on physiochemical and structural properties of polymerized whey proteins (PWP, 10%, w/v) prepared by thermal aggregation at 85°C for 10–30 min. Particle size, zeta potential, isoelectric point (IEP), surface hydrophobicity, free sulphydryl group, rheological properties and the secondary structure of all samples were analysed. ALM pectin increased mean diameter and narrowed size distribution of PWP samples (p < 0.05) regardless of heating time. Addition of ALM pectin shifted the IEP of PWP‒pectin complex to lower pH, which decreased with heating time increased. ALM pectin decreased the surface hydrophobicity of PWP heated for 30 min pronouncedly. Whey protein (WP) complexed with ALM pectin showed decreased gelation time and rheological properties of improved elasticity. ALM pectin had no considerable effect on secondary structure of PWP. Data indicated that ALM pectin could alter physiochemical properties of heat-induced polymerized WPns.

Electrostatic complexes of whey protein and pectin as foaming and emulsifying agents

ABSTRACTFive types of electrostatic complex (macromolecular complexes, core–shell particles, and mixed homogeneous particles) were formed between whey protein (whey protein concentrate [WPC]) and pectin. By controlling the thermal treatment, composition, and order of mixing, it was possible to produce complexes that for the same biopolymer concentration gave differing functional properties. All protein–pectin complexes showed higher foaming ability and stability than native or heated WPC without pectin. Native WPC had higher emulsifying ability than protein–pectin complexes but exhibited the lowest emulsion stability. Ingredients based on such ideas might offer the food manufacturer greater control over food structure, stability, and organoleptic properties.

The influence of pH and enzyme cross-linking on protein delivery properties of WPI-beet pectin complexes

The incorporation of bioactive proteins and peptides into food is associated with the loss of bioactivity due to deactivation in complex food matrices and in digestion systems. In this study, two different types of protein carriers, i.e. biopolymer complexation and complex coacervation were fabricated using whey protein isolation (WPI, 6wt%) and beet pectin (BP, 1.25 and 1.00wt%) at pH5.5 and 3.5, respectively. The release of the encapsulated FITC-BSA, a model bioactive protein, in both carriers in the absence and presence of laccase was investigated at both pH7.0 and 4.0. Release of FITC-BSA from both lyophilized WPI-beet pectin biopolymer complexation and complex coacervation were biphasic with an initial burst release followed by a slower release phase. The addition of laccase in biopolymer complexation increased the loading efficiency from 44.95% to 52.15% and slowed down the burst release of FITC-BSA but did change the biphasic release pattern. Laccase-cross linked WPI (6wt%)-BP (1wt%) complex coacervation had highest FITC-BSA loading efficiency (96.90%). The release of the embedded FITC-BSA in this carrier at both pH4 and 7 was in a gradual manner and the profile can be fit to zero order kinetics over the 72h study period suggesting enzymatically reinforced complex coacervation between the protein and the negatively charged beet pectin can restrain the burst release of FITC-BSA. These results indicate that laccase cross-linked WPI-beet pectin complex coacervation can be a good carrier system for delivering hydrophilic bioactive proteins or peptides successfully with enhanced loading parameters and sustained release profiles.

Relating physicochemical properties of alginate-HMP complexes to their performance as drug delivery systems

This study aims to analyze the effect of physicochemical properties of alginate-high methoxyl pectin (HMP) complexes on their performance as drug delivery systems. Rheology, textural properties and swelling behavior of alginate-HMP complexes were determined. HMP alone showed weak gelling ability. As ratio of alginate increased, gel capability, hardness and adhesiveness of gels increased, but swelling rate decreased. Bovine serum albumin (BSA) was used as a model drug and entrapped in the alginate-HMP beads. Morphology of beads was correlated with adhesiveness. Drug loading content and encapsulation efficiency were related to electrostatic interactions between BSA and alginate-HMP complexes. Drug release profiles were correlated with both texture and swelling properties of alginate-HMP complexes and morphology of beads in simulated gastric fluids, while release in simulated intestinal fluids was affected by drug loading content. This study gives enlightenment that pre-selection of encapsulation materials may be achieved prior to encapsulation based on physicochemical properties of materials.

Optimization of microcapsules shell structure to preserve labile compounds: A comparison between microfluidics and conventional homogenization method

A new technique is presented to optimize the formulation of microcapsules loaded with labile compounds. Fish oil was loaded into the microcapsule core and protected with a shell composed of whey protein microgel/beet pectin complexes. The microcapsules were formed using two different methods: microfluidics and homogenization. The microcapsules were further classified into three sub-groups. The first group was the microcapsules cross-linked with laccase (MCL), the second group was the microcapsules cross-linked with divalent cationic CaCl2 salt (MCS), and the third group consisted of control microcapsules (CM), with no cross-linking. The microfluidics method enabled tracking of the effect of the shell cross-linking ability of laccase, or CaCl2, on microcapsules. It was demonstrated that MCL obtained by microfluidics are more physicochemically stable than those produced via a homogenizer. The effect of cross-linking agents on the microcapsules were more significant when the microcapsules were produced by microfluidics.

Development of double layered emulsion droplets with pectin/β-lactoglobulin complex for bioactive delivery purposes

The objective of the present study was to load piroxicam (PX) into multi-layered oil in water emulsions stabilized by β-lactoglobulin (β-Lg)/pectin complexes. A primary emulsion was produced by homogenizing the sunflower oil contains PX in β-Lg solution (at pH=3.5). Then, the emulsion droplets were stabilized further by coating with pectin as a secondary layer. Four different pectin types including low-methoxyl sunflower pectin (LMSP), high-methoxyl apple pectin (HMAP), high-methoxyl citrus pectin (HMCP), and low-methoxyl citrus pectin (LMCP) were applied for production of double layered emulsion droplets. The entrapping efficiency of PX (%), creaming stability, and mean droplet size (D43) of emulsions were measured. Also, the release trends of PX were determined and fitted with experimental models of zero order, Higuchi, and Pepass. Our results revealed that the emulsions stabilized by β-Lg/high-methoxyl apple and citrus pectins with NaCl had a higher creaming stability and more loading capacity of PX compared to stabilized emulsions by β-Lg/pectin without NaCl. The mean droplet size (D43) of double layered emulsions was increased at higher pectin fraction and were decreased by lower β-lg fraction.

Protection of blue color in a spirulina derived phycocyanin extract from proteolytic and thermal degradation via complexation with beet-pectin

The focus of the presented work was on improvement of spirulina based phycocyanin (PhyC) extracts as a potential natural blue colorant by enhancement of color stability via polysaccharide complexation. Beet pectin (β-pectin), guar gum and soluble soy polysaccharides (SSPS) were assessed for their ability to protect the color of a commercial phycocyanin (PhyC) extract from thermal and proteolytic degradation. Both the beet pectin and guar gum studied formed stable and homogenous solutions with the PhyC extract; SSPS did not. Color change was assessed throughout by measurement of L, a, and b color space values (Hunter, 1948) before and after thermal or proteolytic treatment. Beet pectin improved color stability, over PhyC alone, with respect to heating at 65 °C (20 min) and proteolysis by Alcalase 2.4L, papain and bromelain. For these treatments beet pectin reduced color change values (ΔEab) from 13.0 ± 0.1 to 6.2 ± 0.4 following thermal treatment and from 12.7 ± 0.2 to 5.9 ± 0.7, 19.6 ± 1.3 to 12.5 ± 0.8, and 10.8 ± 0.4 to 4.6 ± 0.6 for the Alcalase, papain and bromelain treatments, respectively. Intrinsic fluorescence (excitation at 285 nm, emission at 325 nm) of beet pectin complexed PhyC indicates an increased presence of exposed tryptophan residues compared to PhyC alone. Furthermore, measured zeta-potentials following complex heating generally diverged to slightly more negative values for PhyC-beet pectin complexes at elevated temperatures compared to PhyC alone, suggesting that maintenance of a negatively charged environment may be important to pigment color stability in PhyC complexes.

Influence of shear stress, pectin type and calcium chloride on the process stability of thermally stabilised whey protein–pectin complexes

There is a strong demand for fat-reduced foods due to an increasing incidence of overweight and obesity. To overcome the sensory deficiencies going along with a fat reduction, process stable fat replacers with tailored properties, such as whey protein–pectin complexes, are necessary. In this study, the effects of process (shear rate: 0, 150, 500 s−1; scale: lab/pilot plant) and composition (pectin type: high/low degree of blockiness; CaCl2: 0, 15, 30 mM; biopolymer concentration: chigh = 5.0% WPI + 1.0% pectin; cmed = 2.75 + 0.55%; clow = 0.5 + 0.1%) parameters on micro- and macro-structural characteristics of whey protein–pectin (WPI–pectin) complexes were investigated. Thermomechanical treatments of WPI–pectin suspensions in a high-pressure double gap geometry revealed a high shear stability during complex generation at 500 s−1. The degree of blockiness (DB) of pectin was identified as critical parameter influencing complex structure and biopolymer system stability. WPI–pectin complexes with a high DB pectin had a fragile structure low DB resulted in a compact structure. The shear rate was the main parameter to adjust yield and particle size, both on the lab and pilot scale. A higher shear rate led to a higher yield consisting of smaller particles. This effect could be partially compensated by medium CaCl2 concentrations (≤10 mM) or high biopolymer concentrations (≤5.0% (w/w) WPI + 1.0% (w/w) pectin). Modelling the parameter effects resulted in sets of processing and composition parameters suitable for the generation of WPI–pectin complexes, owning the potential as fat replacers.

Fabrication, characterization and stability of oil in water nano-emulsions produced by apricot gum-pectin complexes

In this study, the effects of apricot gum-apple pectin (AG/pectin) complex as an emulsifier and stabilizer on the sunflower oil in water nano-emulsion parameters including droplet size, zeta-potential, and the creaming index was investigated. The first independent variables were AG concentration in AG/pectin complex. Applying a 21.4 (w/w) ratio of AG/pectin resulted in nano-emulsions with the highest creaming stability, and most stable droplet size and zeta-potential during 10days storage. Then, droplet size, zeta-potential, and stability of this emulsion (21.4 (w/w) ratio) were further investigated under environmental and process stresses including thermal processing, sonication, and pH changes. Emulsions with smaller droplet sizes, higher zeta-potentials, and higher creaming stability were obtained by applying sonication treatment. A 10min ultrasound treatment with the amplitude of 25% was proposed as the optimum conditions for ultra-sonication. Also, emulsions prepared by AG/pectin ratio of 21.4 (w/w) showed best stability at 60°C and pH of 2.

An oligogalacturonide‐derived molecular probe demonstrates the dynamics of calcium‐mediated pectin complexation in cell walls of tip‐growing structures

Pectic homogalacturonan (HG) is one of the main constituents of plant cell walls. When processed to low degrees of esterification, HG can form complexes with divalent calcium ions. These macromolecular structures (also called egg boxes) play an important role in determining the biomechanics of cell walls and in mediating cell-to-cell adhesion. Current immunological methods enable only steady-state detection of egg box formation insitu. Here we present a tool for efficient real-time visualisation of available sites for HG crosslinking within cell wall microdomains. Our approach is based on calcium-mediated binding of fluorescently tagged long oligogalacturonides (OGs) with endogenous de-esterified HG. We established that more than seven galacturonic acid residues in the HG chain are required to form a stable complex with endogenous HG through calcium complexation insitu, confirming a recently suggested thermodynamic model. Using defined carbohydrate microarrays, we show that the long OG probe binds exclusively to HG that has a very low degree of esterification and in the presence of divalent ions. We used this probe to study real-time dynamics of HG during elongation of Arabidopsis pollen tubes and root hairs. Our results suggest a different spatial organisation of incorporation and processing of HG in the cell walls of these two tip-growing structures.