Study on physicochemical characteristics of lutein nanoemulsions stabilized by chickpea protein isolate-stevioside complex.

BACKGROUND: Chickpea protein isolate (CPI) originating from chickpeas has the advantages of facilitating the stability of food emulsions. Stevioside (STE) exhibits a notable surface activity and can improve the water solubility of numerous hydrophobic nutrients. STE and protein mixtures show great potential as emulsions stabilizers. The present study aimed to prepare a novel nanoemulsion for encapsulating lutein (LUT) by ultrasonic homogenization using chickpea protein isolate-stevioside complex (CPI-STE) as a stabilizer and also to investigate the physicochemical characteristics. RESULTS: The results obtained showed that different preparation conditions demonstrated significant influences on the physicochemical properties of CPI-STE-LUT nanoemulsions. Under the optimal condition, the average particle size of CPI-STE-LUT nanoemulsions was 195.1 nm, and the emulsifying and encapsulation efficiencies of lutein were 91.04% and 87.56%, respectively. CPI-STE-LUT nanoemulsions stabilized by CPI-STE could significantly increase the emulsifying and encapsulation efficiencies of lutein compared to that stabilized by CPI. Fourier transform infrared spectroscopy revealed that hydrogen bond was the main binding force of CPI and lutein, and there was a covalent bond between the two molecules. Furthermore, the stability of CPI-STE-LUT nanoemulsions in gastrointestinal phase was higher than that of CPI-LUT nanoemulsions, which could load lutein more effectively and be more resistant to digestive enzymes. CONCLUSION: The present study reports the physicochemical characterization of CPI-STE-LUT nanoemulsions for the first time. CPI-STE-LUT nanoemulsions were characterized by a small average particle size lower than 200 nm, as well as high emulsifying and encapsulation efficiencies, and good stability. © 2021 Society of Chemical Industry.

Effect of chickpea (Cicer arietinum L.) protein isolate on the heat-induced gelation properties of pork myofibrillar protein.

BACKGROUND: Heat-induced composite gels were prepared with 30 mg mL-1 pork myofibrillar protein (MP) and chickpea protein isolate (CPI) (0, 3, 6, 9, 12, and 15 g kg-1 ) in 0.6 mol L-1 NaCl, at pH 7.0. The gel strength, water-holding capacity, rheological properties, and microstructure of MP-CPI composite gels were investigated. RESULTS: Chickpea protein isolate improved (P < 0.05) gel strength and water-holding capacity of the MP composite gels. The rheological properties of MP-CPI composite gels were improved significantly by the addition of CPI. Meanwhile, the effects of CPI on the storage modulus of composite gels were positively correlated with the increased addition of CPI. Furthermore, according to low-field nuclear magnetic resonance (LF-NMR) results, the addition of CPI reduced the relaxation time of the composite gels and the relaxation peak area of free water, indicating that CPI could improve the water-holding capacity of MP-CPI composite gels. The microstructure of MP-CPI composite gels presented smaller and more uniform pores, which means that more water could be retained. CONCLUSION: The addition of chickpea protein isolate improved the gel strength, water-holding capacity, rheological properties, and microstructure of MP gels, indicating that CPI could be a potential protein additive to improve the microstructure, texture, and functional quality of meat products. © 2020 Society of Chemical Industry.

Study on the structural characteristics and emulsifying properties of chickpea protein isolate-citrus pectin conjugates prepared by Maillard reaction.

Chickpea protein isolate (CPI) typically exhibits limited emulsifying properties under various food processing conditions, including pH variations, different salt concentrations, and elevated temperatures, which limits its applications in the food industry. In this study, CPI-citrus pectin (CP) conjugates were prepared through the Maillard reaction to investigate the influence of various CP concentrations on the structural and emulsifying properties of CPI. With the CPI/CP ratio of 1:2, the degree of graft reached 35.54 %, indicating the successful covalent binding between CPI and CP. FT-IR and intrinsic fluorescence spectroscopy analyses revealed alterations in the secondary and tertiary structures of CPI after glycosylation modification. The solubility of CPI increased from 81.39 % to 89.59 % after glycosylation. Moreover, freshly prepared CPI emulsions showed an increase in interfacial protein adsorption (70.33 % to 92.71 %), a reduction in particle size (5.33 µm to 1.49 µm), and a decrease in zeta-potential (-34.9 mV to -52.5 mV). Simultaneously, the long-term stability of the emulsions was assessed by employing a LUMiSizer stability analyzer. Furthermore, emulsions prepared with CPI:CP 1:2 exhibited excellent stability under various environmental stressors. In conclusion, the results of this study demonstrate that the glycosylation is a valuable approach to improve the emulsifying properties of CPI.

Evaluation of chickpea protein isolate as a partial replacement for phosphate in pork meat batters: Techno-functional properties and molecular characteristic modifications.

The effects of chickpea protein isolate (CPI, 0.5-2 %, w/w) on the techno-functional properties of 50 % reduced-phosphate pork meat batters (RPMBs) were explored. The results showed that 1.5-2 % CPI significantly decreased the cooking loss but significantly increased the emulsion stability, hardness, gumminess, chewiness and yellowness (b*) of RPMBs (P < 0.05). CPI altered molecular characteristics of RPMBs, as demonstrated by the increased storage modulus (G'), the conversion of free water into immobilized water, the reduced intensities of the aliphatic residue Raman bands, the decreased α-helical structure and the formation of well-organized gel networks with evenly distributed small fat globules. Principal component analysis and Pearson's correlation analysis indicated that CPI-induced changes in RPMB techno-functional properties were closely related to molecular characteristics. Hierarchical cluster analysis suggested that RPMBs supplemented with 1.5-2 % CPI were highly similar in techno-functional properties to the high-phosphate group. Therefore, CPI may potentially be used to develop reduced-phosphate meat products.

Inducing the structural interplay of binary pulse protein complex to stimulate the solubilization of chickpea (Cicer arietinum L.) protein isolate.

Chickpea protein (CP) is an exceptional nutrient-dense pulse protein prevailing in the development of plant-based foods. However, its relatively low solubility, compared to other legume proteins, hinders the practical uses of CP in food matrix. To resolve this problem, pea protein (PP), another popular pulse protein, was co-assembled with CP to form a binary complex during the alkaline pH-shifting process. Results indicated that the complexed CP exhibited significantly increased solubility to that of the pristine protein (more than 50%), whose aqueous stability was also enhanced against different environmental stresses (pH, salt, heat/frozen treatment, and centrifugation). Structural and morphology analysis confirmed the interplay between unfolded CP and PP during pH shifting, which enabled their resistance to acid-induced structural over-folding. Our experiments that induce the co-assembling of two pulse proteins provide a novel routine and scientific basis for tailoring CP functionalities, as well as the formulation of pulse protein-based products.

The Stability, Rheological Properties and Interfacial Properties of Oil-in-Water (O/W) Emulsions Prepared from Dielectric Barrier Discharge (DBD) Cold Plasma-Treated Chickpea Protein Isolate and Myofibrillar Protein Complexes.

In order to increase the development and utilization of chickpea protein isolate (CPI) and improve the stability of myofibrillar protein (MP) emulsions, the effect of dielectric barrier discharge (DBD) plasma-modified CPI on the emulsifying properties of MP was investigated. Three different O/W emulsions were prepared using MP, MP + CPI complex, or MP + DBD-treated CPI complex as the emulsifier. Compared with the emulsion prepared from MP, the emulsifying activity index and stability of DBD-treated CPI and MP complex (MP + CPIDBD) were increased (p < 0.05) from 55.17 m2/g to 74.99 m2/g and 66.31% to 99.87%, respectively. MP + CPIDBD produced more stable emulsions with the lowest Turbiscan stability index (TSI) values for a given 3600 s. At shear rates from 0 to 1000-1, MP + CPIDBD-stabilized emulsions had higher viscosities, which helped to reduce the chance of aggregation between oil droplets. The optical microscope and particle size distribution of emulsions showed that MP + CPIDBD emulsions had the lowest droplet size (d4,3) and exhibited more uniform distribution. MP + CPIDBD emulsions had lower interfacial tension. DBD pretreatment increased the adsorbed protein content in the emulsion stabilized by MP + CPIDBD as compared to the MP + CPI complex and promoted the adsorption of CPI by higher ratios of adsorbed proteins as indicated by its intensity in SDS-PAGE. Scanning electron microscopy confirmed that the emulsion prepared from MP + CPIDBD had smaller particle size and more uniform dispersion. Therefore, using DBD-modified CPI could enhance the stability of MP emulsions.

Formulation and characterization of 3D printed chickpea protein isolate-mixed cereal dysphagia diet.

The feasibility study of making 3D printed dysphagia diet was undertaken. A mixture of corn flour and buckwheat flour was used as the model cereal and chickpea protein isolate (CPI) was used as the model protein. Printing gels (inks) of the mixed cereal (control) and CPI-cereal mixture were produced by heating the formulations at 95 °C for 30 min and then cooling them to room temperature. The results showed that all the ink formulations containing CPI had higher apparent viscosity, preferable shear thinning behavior and shape supporting characteristics than that of the control. The cohesiveness and shape supporting ability of 10%CPI-cereal and 20%CPI-cereal formulations were poor and could not produce stable printing shape. The 30%CPI-cereal and 40%CPI-cereal formulations had suitable apparent viscosity, shear thinning behavior, storage modulus, yield stress and printing accuracy and the 3D printed products were stable. The control ink and 10%CPI-cereal ink had low cohesion and also could not pass the spoon tilt test. The 50%CPI-cereal formulation had high hardness and also could not pass the fork pressing test. The 30 % to 40 % CPI-cereal formulations were found to be suitable as dysphagia products as they could be classified as level 5 dysphagia diet.

Deciphering the interaction mechanism and binding mode between chickpea protein isolate and flavonoids based on experimental studies and molecular simulation.

Chickpea protein isolate (CPI) is a promising novel plant protein, and protein-flavonoid system has also been applied in various food products. However, the interaction mechanism between CPI and flavonoids remains to be elucidated. In this paper, the affinity behavior between flavonoids and CPI was explained by constructing the three-dimensional quantitative structure-activity relationship (R2 = 0.988, Q2 = 0.777). Subsequently, four representative flavonoids were selected for further study. Multi-spectroscopy analysis showed that the sequence of affinity for CPI was puerarin > apigenin > naringenin > epigallocatechin gallate. Meanwhile, flavonoids altered the secondary structure and spatial conformation of CPI, leading to the static quenching of CPI. Additionally, thermodynamic analysis indicated that hydrogen bonding and van der Waals forces were the main driving forces for complex binding. Molecular docking and molecular dynamics simulations further explored the binding sites and conformations of complexes. This study provides theoretical guidance for in-depth research on the interaction patterns between biomacromolecules and small molecules in food matrices.

Influence of atmospheric pressure plasma jet on the structural, functional and digestive properties of chickpea protein isolate.

Chickpea protein (CPI) is a promising dietary protein and potential substitute for soy protein in food product development due to its high protein content and low allergenicity. However, CPI possesses denser tertiary and quaternary structures and contains certain amount of anti-nutritional factors, both of which constrain its functional properties and digestibility. The objective of this study was to assess the effectiveness of atmospheric pressure plasma jets (APPJ) as a non-thermal method for enhancing the functional characteristics and digestibility of CPI. In this study, the reactive oxygen and nitrogen species generated by the APPJ treatment led to protein oxidation and increased carbonyl and di-tyrosine contents. At the same time, the secondary, tertiary and microstructural structures of CPI were changed. The solubility, water holding capacity, fat absorption capacity, emulsifying capacity and foaming capacity of CPI were significantly improved after 30 s APPJ treatment, and a higher storage modulus in rheology was observed. Additionally, it was observed that the in vitro protein digestibility (IVPD) of APPJ-treated CPI increased significantly from 44.85 ± 0.6 % to 50.2 ± 0.59 % following in vitro simulated gastric and intestinal digestion, marking a noteworthy improvement of 11.93 %. These findings indicate that APPJ processing can enhance the functional and digestive properties of CPI through structural modification and expand its potential applications within the food industry.

Effects of combined chickpea protein isolate and chitosan on the improvement of technological quality in phosphate-free pork meat emulsions: Its relation to modifications on protein thermal and structural properties.

The effects of combined chickpea protein isolate (CPI, 1%, w/w) and chitosan (CHI, 1%, w/w) on the technological, thermal, and structural properties of phosphate-free pork meat emulsions (PPMEs) were investigated. The results showed that CPI + CHI significantly improved the emulsion stability (P < 0.05), synergistically elevated the hardness and chewiness, and did not negatively impact the color attributes, which endowed the PPMEs with similar or even better technological performances compared to the high-phosphate control. These alterations were related to the reduced myosin enthalpy values, the rearrangement of free water into immobilized water, the synergistic reduction in α-helical structure and increase in ß-sheet structure, the increased trans-gauche-trans SS conformation intensity of the Raman bands, and the formation of interactive protein gel networks where small-sized fat particles were evenly dispersed in the protein matrix. Therefore, combined CPI and CHI shows promise as a phosphate replacer for meat products.

Transglutaminase-Induced Polymerization of Pea and Chickpea Protein to Enhance Functionality.

Pulse proteins, such as pea and chickpea proteins, have inferior functionality, specifically gelation, compared to soy protein, hindering their applications in different food products, such as meat analogs. To close the functionality gap, protein polymerization via targeted modification can be pursued. Accordingly, transglutaminase-induced polymerization was evaluated in pea protein isolate (PPI) and chickpea protein isolate (ChPI) to improve their functionality. The PPI and ChPI were produced following a scaled-up salt extraction coupled with ultrafiltration (SE-UF) process. Transglutaminase (TGase)-modified PPI and ChPI were evaluated in comparison to unmodified counterparts and to commercial protein ingredients. Protein denaturation and polymerization were observed in the TG PPI and TG ChPI. In addition, the TGase modification led to the formation of intermolecular ß-sheet and ß-turn structures that contributed to an increase in high-molecular-weight polymers, which, in turn, significantly improved the gel strength. The TG ChPI had a significantly higher gel strength but a lower emulsification capacity than the TG PPI. These results demonstrated the impact of the inherent differences in the protein fractions on the functional behavior among species. For the first time, the functional behavior of the PPI and ChPI, produced on a pilot scale under mild processing conditions, was comprehensively evaluated as impacted by the TGase-induced structural changes.

Salt Solubilization Coupled with Membrane Filtration-Impact on the Structure/Function of Chickpea Compared to Pea Protein.

The demand for pulse proteins as alternatives to soy protein has been steeply increasing over the past decade. However, the relatively inferior functionality compared to soy protein is hindering the expanded use of pulse proteins, namely pea and chickpea protein, in various applications. Harsh extraction and processing conditions adversely impact the functional performance of pea and chickpea protein. Therefore, a mild protein extraction method involving salt extraction coupled with ultrafiltration (SE-UF) was evaluated for the production of chickpea protein isolate (ChPI). The produced ChPI was compared to pea protein isolate (PPI) produced following the same extraction method in terms of functionality and feasibility of scaling. Scaled-up (SU) ChPI and PPI were produced under industrially relevant settings and evaluated in comparison to commercial pea, soy, and chickpea protein ingredients. Controlled scaled-up production of the isolates resulted in mild changes in protein structural characteristics and comparable or improved functional properties. Partial denaturation, modest polymerization, and increased surface hydrophobicity were observed in SU ChPI and PPI compared to the benchtop counterparts. The unique structural characteristics of SU ChPI, including its ratio of surface hydrophobicity and charge, contributed to superior solubility at both a neutral and acidic pH compared to both commercial soy protein and pea protein isolates (cSPI and cPPI) and significantly outperformed cPPI in terms of gel strength. These findings demonstrated both the promising scalability of SE-UF and the potential of ChPI as a functional plant protein ingredient.

Effects of Ultrasonic Treatment on the Structure, Functional Properties of Chickpea Protein Isolate and Its Digestibility In Vitro.

This study evaluated the effects of different levels of ultrasonic power (200, 400, 600 W) and treatment time (0, 10, 15 and 30 min) on the structure, emulsification characteristics, and in vitro digestibility of chickpea protein isolate (CPI). The changes in surface hydrophobicity of CPI indicated that ultrasound treatment exposed more hydrophobic amino acid residues. The analysis of sulfhydryl content and zeta potential showed that ultrasound caused the disulfide bond of CPI to be opened, releasing more negatively charged groups, and the solution was more stable. In addition, Fourier Transform Infrared Spectroscopy (FT-IR) and intrinsic fluorescence spectroscopy showed that ultrasound changes the secondary and tertiary structure of CPI, which is due to molecular expansion and stretching, exposing internal hydrophobic groups. The emulsification and foaming stability of CPI were significantly improved after ultrasonic treatment. Ultrasonic treatment had a minor effect on the solubility, foaming capacity and in vitro digestibility of CPI. All the results revealed that the ultrasound was a promising way to improve the functional properties of CPI.

Effects of oxidative modification of peroxyl radicals on the structure and foamability of chickpea protein isolates.

A chickpea protein isolate (CPI) was oxidized using peroxyl radicals derived from 2,2'-azobis (2-amidopropane) dihydrochloride (AAPH), and the structural and foaming properties of the oxidized CPI were evaluated. The oxidation degree of protein was determined by measuring carbonyl content, dimer tyrosine content, free thiol content, and total thiol content. The structural changes of oxidized protein were evaluated by surface hydrophobicity, endogenous fluorescence intensity, Fourier transform infrared spectroscopy, SDS-PAGE, and amino acid content changes. Compared with the control group (0 mmol/L AAPH), moderate oxidation (0.04 mmol/L AAPH) led to the formation of a soluble protein with flexibility, which could improve the foaming properties of the protein (foaming capacity and stability increased by 25.50% and 6.38%, respectively). Over-oxidized (25 mmol/L AAPH) protein exhibited improved foaming capability, but its foam stability was reduced owing to the formation of insoluble aggregates. The results indicate that oxidation can change protein conformation, and the protein structure can affect the foamability of the CPI. PRACTICAL APPLICATION: CPI is a protein supplement food. Protein oxidation can occur during processing and storage, thereby affecting protein function. In this study, we evaluated how peroxy free radicals affect the structure, solubility and foaming properties of CPI, and clarified the mechanism between them. It has been found that peroxy free radicals can accelerate the oxidation of proteins and have a significant effect on foaming. Therefore, the degree of oxidation should be controlled to improve the quality of CPI.

Utilization of chickpea protein isolate and Persian gum for microencapsulation of licorice root extract towards its incorporation into functional foods.

This study aimed at the fabrication of licorice extract (LE)-loaded microparticles by complex coacervation, using chickpea protein isolate (CPI) and soluble fraction of Persian gum (SFPG). The LE-loaded microparticles with the highest encapsulation efficiency (97.87%) and loading capacity (11.35%) were obtained at pH 3 and CPI: SFPG ratio, core: coating ratio, and polymer concentration of 2, 1.5, and 2, respectively. The LE-loaded microparticles (2-15 µm) possessed heterogeneous microstructure, and the Fourier-transform infrared spectroscopy data confirmed the pronounced effect of electrostatic interactions and hydrogen bonding. The thermostability, amorphous structure, and color of the LE-loaded microparticles were significantly enhanced, compared to free LE. The sensory evaluation of the model beverages containing LE-loaded microparticles revealed that the microencapsulation was able to mask the bitter aftertaste and color of the extract. Thus, the results of this research confirm the potential of CPI-SFPG complex coacervates for the efficient delivery of glycyrrhizin via incorporation into functional food products.

Effect of germination, roasting, and variety on physicochemical, techno-functional, and antioxidant properties of chickpea (Cicer arietinum L.) protein isolate powder.

Chickpeas are a very important part of the human diet due to their nutritional and bioactive composition. Ethiopia is one of the top chickpea producers and consumers of chickpea-based products daily. However, limited studies were conducted on the effect of common processing methods, roasting and germination, on techno-functional and nutritional properties of chickpea protein isolates. Two varieties of chickpea, Arerti (Kabuli type) and Natoli (Desi type), were selected and treated with different roasting temperature (150 and 180 °C) and germination time (24, 48, and 72 h). The protein was isolated with alkaline-solubilization followed by isoelectric precipitation. Freeze-dried isolates were investigated for proximate composition, techno-functional properties, antioxidant properties, and antinutritional content. Chickpea protein isolates (CPIs) mean protein content was between 79.72 and 87.43%, comparatively lower for those from roasted and higher for those from germinated chickpea. Mean values of CPIs' water holding capacity (WHC), oil holding capacity (OHC), protein solubility (PS), foaming capacity (FC), and Emulsifying capacity (EC) for both varieties were in a range of 1.07-2.47 g/g, 1.40-2.21 g/g, 43.88-69.99%, 14.00-94.00%, and 56.44-84.16%, respectively. Roasting at 150 °C improved most of the techno-functional properties (WHC, OHC, PS, and FC) while roasting at 180 °C negatively affected almost all the techno-functional properties. Both heat treatments significantly increased the antioxidant properties of the isolates. Germination for 72 h was the best treatment in improving all antioxidant properties. CPIs from treated chickpea had lower antinutritional content than those from native chickpea except for phytate on Natoli variety where no statistical difference (p > 0.05) was observed. The finding showed that based on the intended use the different techno-functional properties of the isolates can be altered by applying those treatments. Proximate, techno-functional, antioxidant, and antinutritional characters indicated that CPIs can be a good ingredient for the food industry to formulate functional foods.

Effects of Chickpea Protein on Carbohydrate Reactivity in Acrylamide Formation in Low Humidity Model Systems.

Asparagine and reducing sugars are the principal precursors of acrylamide in foods. Their main sources in pastries are flour and hen egg yolks. One method of reducing acrylamide content in food may be to add a chickpea protein preparation. The aim of the study was to determine the effects of the chickpea protein preparation on the thermodynamic properties of carbohydrates and the amount of acrylamide formed in low humidity model systems. In the studied systems, the type and amount of acrylamide precursors and humidity were designed to reflect the parameters typical of shortcrust cookies. In the study, the highest amounts of acrylamide were formed in the reaction between asparagine and fructose and the lowest in the reaction between asparagine and sucrose. Furthermore, the addition of chickpea protein to the analyzed carbohydrate-asparagine model systems reduced the content of acrylamide formed during baking at 180 °C regardless of the type of carbohydrate. The greatest acrylamide reduction (41%) was found in the model system containing fructose.

Functional properties of chickpea protein isolates dried by refractance window drying.

In the present study, the effect of Refractance Window (RW) drying on the functional properties of chickpea protein isolates was investigated and compared to freeze drying at different pH levels. The functional properties investigated were protein solubility, water and oil holding capacity, emulsifying properties, foaming properties, flocculation and coalescence indices and textural properties. The solubility, oil holding capacity and foam stability of the freeze dried protein isolates were determined to be higher than the RW dried samples. On the other hand, the RW dried samples had better water holding capacity and emulsion stability compared to the freeze dried protein isolates. The emulsion activity index, flocculation and coalescence indices of the chickpea protein isolates prepared by different drying techniques showed different tendencies depending on the pH level. Freeze dried protein isolates exhibited higher gelation ability than RW dried samples according to the texture profile analysis. This study clearly showed that the drying technique used in the preparation of protein isolates can affect their functional properties.