Combined high voltage atmospheric cold plasma and ultraviolet-cold plasma inhibited Aspergillus flavus growth and improved physicochemical properties of protein in peanuts.

To improve the application value of peanuts, the fungicidal effect and physicochemical properties of the protein in peanuts were investigated by combining high voltage atmospheric cold plasma (HVCP) and ultraviolet-cold plasma (UVCP) in this study. Compared to the single HVCP or UVCP treatment, the combined treatments exhibited a higher fungicidal efficiency of A. flavus spores in peanuts, decreasing by 0.79-2.97 log10 cfu/g after 8-min treatment. The A. flavus growth and aflatoxin production in peanuts during storage were also lower than the single plasma groups. Moreover, cold plasma treatments could modify the molecular structures of protein in peanuts by changing secondary and tertiary structures, decreasing particle size and increasing zeta potential, which contributed to improve the solubility and emulsification of protein. Overall, this research provides a unique strategy for the combined application of cold plasma in grain decontamination and protein modification.

Interactions with peanut protein isolate regulate the bioaccessibility of cyanidin-3-O-glucoside: Multispectral analysis, simulated digestion, and molecular dynamic simulation.

Anthocyanins are susceptible to degradation owing to environmental factors. Combining them with proteins can improve their stability; however, the interaction mechanism is difficult to elucidate. This study used multispectral and molecular dynamics simulations and molecular docking methods to investigate the interaction mechanism between peanut protein isolate (PPI) and cyanidin-3-O-glucoside (C3G). The UV absorption peak and PPI turbidity increased, while the fluorescence intensity decreased with greater C3G content. Protein secondary structure changes suggested that PPI and C3G coexisted in spontaneous covalent and non-covalent interactions via static quenching. The complex structures were stable over time and C3G stably bound to the peanut globulin Ara h 3 cavity through hydrogen bonding and hydrophobic interactions. Furthermore, PPI enhanced the C3G antioxidant activity and bioaccessibility by increasing its retention rate during in-vitro simulated digestion. This study elucidates the binding mechanism of PPI and C3G and provides insight into applications of the complex in food development.

Comparison of intestinal absorption of soybean protein isolate-, glutenin- and peanut protein isolate-bound Nε-(carboxymethyl) lysine after in vitro gastrointestinal digestion.

Advanced glycation end products (AGEs), a heterogeneous compound existed in processed foods, are related to chronic diseases when they are accumulated excessively in human organs. Protein-bound Nε-(carboxymethyl) lysine (CML) as a typical AGE, is widely determined to evaluate AGEs level in foods and in vivo. This study investigated the intestinal absorption of three protein-bound CML originated from main food raw materials (soybean, wheat and peanut). After in vitro gastrointestinal digestion, the three protein-bound CML digests were ultrafiltered and divided into four fractions: less than 1 kDa, between 1 and 3 kDa, between 3 and 5 kDa, greater than 5 kDa. Caco-2 cell monolayer model was further used to evaluate the intestinal absorption of these components. Results showed that the absorption rates of soybean protein isolate (SPI)-, glutenin (Glu)-, peanut protein isolate (PPI)-bound CML were 30.18%, 31.57% and 29.5%, respectively. The absorption rates of components with MW less than 5 kDa accounted for 19.91% (SPI-bound CML), 22.59% (Glu-bound CML), 23.64% (PPI-bound CML), respectively, and these samples were absorbed by paracellular route, transcytosis route and active route via PepT-1. Taken together, these findings demonstrated that all three protein-bound CML digests with different MW can be absorbed in diverse absorption pathways by Caco-2 cell monolayer model. This research provided a theoretical basis for scientific evaluation of digestion and absorption of AGEs in food.

Effects of enzymatic hydrolysis combined with glycation on the emulsification characteristics and emulsion stability of peanut protein isolate.

Peanut protein isolate (PPI) has high nutritional value, but its poor function limits its application in the food industry. In this study, peanut protein isolate was modified by enzymatic hydrolysis combined with glycation. The structure, emulsification and interface properties of peanut protein isolate hydrolysate (HPPI) and dextran (Dex) conjugate (HPPI-Dex) were studied. In addition, the physicochemical properties, rheological properties, and stability of the emulsion were also investigated. The results showed that the graft degree increased with the increase of Dex ratio. Fourier transform infrared spectroscopy (FTIR) confirmed that the glycation of HPPI and Dex occurred. The microstructure showed that the structure of HPPI-Dex was expanded, and the molecular flexibility was enhanced. When the ratio of HPPI to Dex was 1:3, the emulsifying activity and the interface pressure of glycated HPPI reached the highest value, and the emulsifying activity (61.08 m2/g) of HPPI-Dex was 5.28 times that of PPI. The HPPI-Dex stabilized emulsions had good physicochemical properties and rheological properties. In addition, HPPI-Dex stabilized emulsions had high stability under heat treatment, salt ion treatment and freeze-thaw cycle. According to confocal laser scanning microscopy (CLSM), the dispersion of HPPI-Dex stabilized emulsions was better after 28 days of storage. This study provides a theoretical basis for developing peanut protein emulsifier and further expanding the application of peanut protein in food industry.

Angiotensin-Converting Enzyme and Renin-Inhibitory Activities of Protein Hydrolysates Produced by Alcalase Hydrolysis of Peanut Protein.

Hypertension is a major controllable risk factor associated with cardiovascular disease (CVD) and overall mortality worldwide. Most people with hypertension must take medications that are effective in blood pressure management but cause many side effects. Thus, it is important to explore safer antihypertensive alternatives to regulate blood pressure. In this study, peanut protein concentrate (PPC) was hydrolyzed with 3-5% Alcalase for 3-10 h. The in vitro angiotensin-converting enzyme (ACE) and renin-inhibitory activities of the resulting peanut protein hydrolysate (PPH) samples and their fractions of different molecular weight ranges were determined as two measures of their antihypertensive potentials. The results show that the crude PPH produced at 4% Alcalase for 6 h of hydrolysis had the highest ACE-inhibitory activity with IC50 being 5.45 mg/mL. The PPH samples produced with 3-5% Alcalase hydrolysis for 6-8 h also displayed substantial renin-inhibitory activities, which is a great advantage over the animal protein-derived bioactive peptides or hydrolysate. Remarkably higher ACE- and renin-inhibitory activities were observed in fractions smaller than 5 kDa with IC50 being 0.85 and 1.78 mg/mL. Hence, the PPH and its small molecular fraction produced under proper Alcalase hydrolysis conditions have great potential to serve as a cost-effective anti-hypertensive ingredient for blood pressure management.

Assessment of Peanut Protein Powder Quality by Near-Infrared Spectroscopy and Generalized Regression Neural Network-Based Approach.

The global demand for protein is on an upward trajectory, and peanut protein powder has emerged as a significant player, owing to its affordability and high quality, with great future market potential. However, the industry currently lacks efficient methods for rapid quality testing. This research paper addressed this gap by introducing a portable device with employed near-infrared spectroscopy (NIR) to quickly assess the quality of peanut protein powder. The principal component analysis (PCA), partial least squares (PLS), and generalized regression neural network (GRNN) methods were used to construct the model to further enhance the accuracy and efficiency of the device. The results demonstrated that the newly established NIR method with PLS and GRNN analysis simultaneously predicted the fat, protein, and moisture of peanut protein powder. The GRNN model showed better predictive performance than the PLS model, the correlation coefficient in calibration (Rcal) of the fat, the protein, and the moisture of peanut protein powder were 0.995, 0.990, and 0.990, respectively, and the residual prediction deviation (RPD) were 10.82, 10.03, and 8.41, respectively. The findings unveiled that the portable NIR spectroscopic equipment combined with the GRNN method achieved rapid quantitative analysis of peanut protein powder. This advancement holds a significant application of this device for the industry, potentially revolutionizing quality testing procedures and ensuring the consistent delivery of high-quality products to fulfil consumer desires.

Effects of different polysaccharide colloids on the structure and physicochemical properties of peanut protein and wheat gluten composite system under extrusion.

The structure and physicochemical properties of the complex system of peanut protein and gluten with different concentrations (0 %, 0.5 %, 1 %, and 2 %) of carboxymethyl cellulose (CMC) or sodium alginate (SA) under high-moisture extrusion were studied. The water absorption index and low-field nuclear magnetic resonance showed that adding 0.5 % SA could significantly improve the water uniformity of peanut protein extrudates, while the increase in water absorption was not significant. The texture properties showed that adding CMC or SA increased the hardness, vertical shearing force, and parallel shearing force of the system. Furthermore, adding 0.5 % SA increased approximately 33 % and 75.2 % of the tensile distance and strength of the system, respectively. The secondary structure showed that CMC or SA decreased the proportion of α-helix, ß-turn, and random coil, while increased ß-sheet proportion. The results of hydrophobicity, unextractable protein, and endogenous fluorescence revealed that CMC and SA reduced the surface hydrophobicity of the system and caused fluorescence quenching in the system. Additionally, it was found that CMC generally increased the free sulfhydryl group content, while SA exhibited the opposite effect.

Studies on the Increasing Saltiness and Antioxidant Effects of Peanut Protein Maillard Reaction Products.

The salt taste-enhancing and antioxidant effect of the Maillard reaction on peanut protein hydrolysates (PPH) was explored. The multi-spectroscopic and sensory analysis results showed that the Maillard reaction products (MRPs) of hexose (glucose and galactose) had slower reaction rates than those of pentose (xylose and arabinose), but stronger umami and increasing saltiness effects. The Maillard reaction can improve the flavor of PPH, and the galactose-Maillard reaction product (Ga-MRP) has the best umami and salinity-enhancing effects. The measured molecular weight of Ga-MRP were all below 3000 Da, among which the molecular weights between 500-3000 Da accounted for 46.7%. The products produced during the Maillard reaction process resulted in a decrease in brightness and an increase in red value of Ga-MRP. The amino acid analysis results revealed that compared with PPH, the content of salty and umami amino acids in Ga-MRPs decreased, but their proportion in total free amino acids increased, and the content of bitter amino acids decreased. In addition, the Maillard reaction enhances the reducing ability, DPPH radical scavenging ability, and Fe2+ chelating ability of PPH. Therefore, the Maillard reaction product of peanut protein can be expected to be used as a substitute for salt seasoning, with excellent antioxidant properties.

Effect of Starch Types on the Textural and Rehydration Properties of Extruded Peanut Protein Pore Gel Particles.

In this study, the effect of different starches from corn, potato and pea containing varying amylose/amylopectin ratios on the textural and rehydration properties of extruded peanut protein gel particles were investigated. Results showed that textural and rehydration properties of peanut protein extruded with corn starch, potato starch and amylopectin are slightly inferior to those of peanut protein with pea starch extrudates. The addition of pea starch led to an increase in the pore structure of the peanut protein extrudates and improved their water absorption index, simultaneously reducing the hardness and density. Pea starch, as a natural water-absorbing expansion material, helped peanut protein to form cross-linked gel polymers that bind more water molecules, in addition to further polymerization with peanut protein, which made the protein secondary structure became disordered. These changes directly affected the textural properties of the extrudates. In addition, the blended system of starches and peanut protein tended to form more elastic solids, which affected the expansion of the extrudates. These findings indicate that starch can effectively improve the poor expansion of proteins, making it suitable for use in the production of plant protein-based foods.

From Skin to Solution: Exploring Epicutaneous Immunotherapy for Peanut Allergy-A Systematic Review and Meta-Analysis.

Peanut allergy is a leading cause of severe food reactions. This meta-analysis evaluates the efficacy and safety of epicutaneous immunotherapy (EPIT) compared to placebo for peanut-allergic individuals. After prospectively registering on PROSPERO, we searched three databases (PubMed, Google Scholar, and Cochrane CENTRAL) and 2 trial registries till September 2023. Analysis was conducted via RevMan where data was computed using risk ratios (RR). The Cochrane Risk of Bias tool and GRADE criteria were used to appraise and evaluate the evidence. From 4927 records, six multicenter randomized placebo-controlled trials comprising 1453 participants were included. The 250 µg EPIT group had a significant increase in successful desensitization compared to placebo (RR: 2.13 (95% C.I: 1.72, 2.64), P < 0.01, I2 = 0%), while the 100 µg EPIT group did not (RR: 1.54 (95% C.I: 0.92, 2.58), P = 0.10, I2 = 0%) (moderate certainty evidence). Moreover, there was a significant increase in local (RR: 1.69 (95% C.I: 1.06, 2.68), P = 0.03, I2 = 89%) and systemic adverse events (RR: 1.75 (95% C.I: 1.14, 2.69), P = 0.01, I2 = 0%) with EPIT. Additionally, individuals administered EPIT have an increased probability of requiring rescue medications like epinephrine (RR: 1.91 (95% C.I: 1.12, 3.28), P = 0.02, I2 = 0%) and topical corticosteroids (RR: 1.49 (95% C.I: 1.29, 1.73), P < 0.01, I2 = 0%) to treat adverse events. The association of adverse events post-treatment including anaphylaxis (RR: 2.31 (95% C.I: 1.00, 5.33), P = 0.05, I2 = 36%), skin/subcutaneous disorders like erythema or vesicles (RR: 0.93 (95% C.I: 0.79, 1.08), P = 0.33, I2 = 0%), and respiratory disorders like dyspnea or wheezing (RR: 0.94 (95% C.I: 0.77, 1.15), P = 0.55, I2 = 0%) with EPIT is inconclusive. EPIT, although effective in desensitization, is linked to an increased risk of adverse events. PROSPERO registration: CRD42023466600.

Influence of carboxymethyl cellulose on the stability, rheology, and curcumin bioaccessibility of high internal phase Pickering emulsions.

Recently, there has been a focus on using biopolymer-based particles to stabilize high internal phase Pickering emulsions (HIPPEs) due to the notable advances in biocompatibility and biodegradability. In this work, the complex particles of peanut protein isolate and carboxymethyl cellulose (CMC) with various substitution degrees (DS; 0.7 and 0.9) and weight average molecular weights (Mw; 90, 250, and 700 kDa) were prepared and characterized as novel stabilizers. For the obtained four types of morphologically distinct particles, the complex particles formed by CMC (0.9 DS and 250 kDa) showed cluster structures with an average size of 1.271 µm, equally biphasic wettability with three-phase contact angles of 91.5°, and the highest diffusion rate at the oil-water interface. HIPPEs stabilized by these particles exhibited more elastic behavior due to the smaller tanδ and higher viscosity, as well as excellent thixotropic recovery properties and stability against heating, storage, and freeze-thawing. Furthermore, confocal laser scanning microscopy verified that these particles formed a dense interfacial layer around the oil droplets, which could resist flocculation and coalescence between oil droplets during in vitro digestion. The improved bioaccessibility of curcumin-loaded HIPPEs made these delivery systems potentially apply in functional foods.

Fat analogue emulsions stabilized by peanut protein microgel particles: microscale and nanoscale structure and stabilization process analysis.

BACKGROUND: Biopolymer-based microgels are being regarded increasingly as promising building blocks in food applications. This study aimed to clarify the evolution process of the network for fat analogue emulsions stabilized by peanut protein isolate (PPI) microgel particles. It also investigated the interfacial structure and characteristics of emulsions (50% oil phase, w/w) stabilized by microgels under different pH conditions. RESULTS: There was an increasing interfacial adsorption capacity for PPI microgels over time (from 85.26% to the maximum of 89.78% at 24 h of storage) due to the aggregation of microgels around droplets and the development of cross-linking microgel chains between adjacent interfaces. The increased ß-sheet content (from 35.51% to 41.12%) of adsorbed microgels indicated unfolding and the enhanced aggregation of microgels, which led to stronger droplet interaction. The network evolution observed with different microscopes clarified the transition to a self-supporting emulsion. The uneven adsorption of large microgel aggregates at the oil-water interface promoted larger and deformed droplets, so more fat-like medium internal phase emulsion stabilized by PPI microgel could be obtained by adjusting the microgel pH to 4.5. The interfacial membranes observed by scanning electron microscopy were thicker and coarser at pH 3.0 and 4.5 than those at pH 7.0 and 9.0. The adsorption of PPI microgel aggregates enhanced the structural strength and improved emulsion stability. CONCLUSION: This work could form a basis for further studies relating physical properties to the design of plant protein-based fat analogues. © 2024 Society of Chemical Industry.

Identification and in vitro Characterization of Novel Antidiabetic Peptides Released Enzymatically from Peanut Protein.

Bioactive peptides derived from proteins found in various foods provide significant health benefits, including regulating blood sugar levels by inhibiting carbohydrate-hydrolyzing enzymes. Hydrolysates of peanut protein were prepared using alcalase (AH) or trypsin (TH) to generate antidiabetic peptides with high activity against α-amylase (IC50 of 6.46 and 5.71 mg/mL) and α-glucosidase (IC50 of 6.30 and 5.57 mg/mL), as well as antiradical activity to scavenge DPPH• (IC50 of 4.18 and 3.12 mg/mL) and ABTS•+ (IC50 of 2.87 and 2.56 mg/mL), respectively. The bioactivities of hydrolysates were greatest in the ultrafiltration-generated F3 fraction (< 3 kDa). The most active fraction was TH-F3, which was purified by gel filtration chromatography to generate sub-fractions (SF). With IC50 values of 1.05 and 0.69 mg/mL, the F3-SF8 fraction was the most effective at inhibiting the activity of α-amylase and α-glucosidase, respectively. This fraction was further purified using RP-HPLC to generate sub-subfractions (SSF), the most active of which were F3-SF8-SSF9 and SSF10. The peptide sequences F3-SF8-SSF9 and SSF10 were determined using LC-MS/MS. Two novel antidiabetic peptides with the potential to inhibit α-amylase and α-glucosidase were identified, with the sequences Asp-Trp-Arg (476.22 Da, IC50 of 0.78, and 0.35 mg/mL) and Phe-Tyr (329.15 Da, IC50 of 0.91, and 0.41 mg/mL). These results suggest that peptides derived from peanut protein are attractive natural ingredients for diabetes management applications.

Changes in the structure and hydration properties of high-temperature peanut protein induced by cold plasma oxidation.

To improve the hydration properties of high-temperature pressed peanut protein isolate (HPPI), we investigated the effect of cold plasma (CP) oxidation on functional and structural properties. Compared to HPPI, the hydrated molecules number and the surface contact angle were significantly decreased at 70 W, from 77.2 × 109 to 17.7 × 109 and from 85.74° to 57.81°, respectively. The reduction of the sulfhydryl content and the increase of the disulfide bond and di-tyrosine content indicated that the structural transformation was affected by the oxidation effect. In terms of structural changes, a stretched tertiary structure, ordered secondary structure, and rough apparent structure were observed after CP treatment. Additionally, the enhancement of surface free energy and group content such as -COOH, -CO and -OH on the surface of HPPI contributed to the formation of hydrated crystal structures. In general, the oxidation effect of CP effectively improved the hydration properties of HPPI and broaden its application field.

Physiochemical characteristics and sensory properties of plant protein isolates-konjac glucomannan compound gels.

In this study, the effects of konjac glucomannan (KGM) at different concentrations on the physiochemical and sensory properties of soy protein isolate (SPI), pea protein isolate (PPI), or peanut protein isolate (PNPI) compound gels were investigated. The results revealed that when the ratio of PNPI to KGM was 90:10, the denaturation temperature of PNPI could be significantly enhanced to 119.32°C by KGM modification. Concerning the textural and microstructural features, the amount of KGM addition had positive correlation with the hardness and chewiness of each compound gel, however, too much KGM addition will cause the unstable internal structure of the PNPI/KGM compound gels (70:30 and 60:40). Furthermore, sensory results indicated that PNPI/KGM (80:20), PPI/KGM (80:20), SPI/KGM (80:20) had great potential to be considered as prototypes for novel plant-based products, which generated the highest acceptance scores of 5.04, 5.94, and 5.36 in each group, respectively.

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 (5.43 W/cm3, 25 min, 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.

IgE Recognition and Structural Analysis of Disulfide Bond Rearrangement and Chemical Modifications in Allergen Aggregations in Roasted Peanuts.

Given that roasting changes the structure and allergenicity of peanut allergens, the structural information of peanut allergens must be expounded to explain the alteration in their allergenicity. This work focused on allergen aggregations (AAs) in roasted peanuts. IgE recognition capability was assessed via western blot analysis. The disulfide bond (DB) rearrangement and chemical modification in AAs were identified by combining mass spectroscopy and software tools, and structural changes induced by cross-links were displayed by molecular dynamics and PyMOL software. Results showed that AAs were strongly recognized by IgE and cross-linked mainly by DBs. The types of DB rearrangement in AAs included interprotein (98 peptide pairs), intraprotein (22 peptide pairs), and loop-linked (6 peptides) DBs. Among allergens, Ara h 2 and Ara h 6 presented the most cysteine residues to cross-linkf with others or themselves. DB rearrangement involved IgE epitopes and induced structural changes. Ara h 1 and Ara h 3 were predominantly chemically modified. Moreover, chemical modification altered the local structures of proteins, which may change the allergenic potential of allergens.

The droplet breakup model and characteristics of pH-shifted peanut protein isolate-high methoxyl pectin stabilised emulsions under ultrasound.

The effect of pH on the occurrence states of peanut protein isolate (PPI) and high methoxyl pectin (HMP), and droplet breakup model of the emulsions under ultrasound were studied. Particle size distribution and scanning electron microscopy results showed that PPI-HMP existed a soluble complex at pH 5.0, had no interaction at pH 7.0, and was co-soluble at pH 9.0. Droplet breakup model results revealed that the characteristics of emulsion stabilised by PPI-HMP treated at pH 5.0 was different from that at pH 7.0 and 9.0. The average diameter of the droplet well satisfied the model. According to rheological properties, interface tension, and microstructure, the formation mechanism and characteristics of emulsion stabilised by PPI-HMP treated at pH 5.0 was different from that at pH 7.0 and pH 9.0. The research provided a reference for constructing emulsions using pH-shifted PPI-HMP under ultrasound.

Modulating the allergenicity and functional properties of peanut protein by covalent conjugation with polyphenols.

Peanut protein is a common food allergen. Our previous study demonstrated that the allergenicity of Ara h1 declines after covalent conjugation with polyphenols in vitro; however, how polyphenols affect the structure, function, and allergenicity of peanut protein extract (PPE) after covalent conjugating needs clarifying. Here, we assessed how the structure, function, and allergenicity of PPE changed after covalent conjugation with epigallocatechin-3-gallate (PPE-EGCG) and chlorogenic acid (PPE-CA). PPE covalently conjugated with EGCG and CA using the alkali treatment method. Multi-spectroscopy showed that the structure of PPE-EGCG/CA conjugate changed, becoming less folded. In contrast, the functional properties of PPE significantly improved. The allergenicity of PPE-EGCG/CA significantly declined in vitro and in vivo experiments. Our findings confirm that covalent conjugation of PPE with EGCG and CA reduces the allergenicity and improves the functional properties of PPE by changing the structure of the protein.

Impact of interactions between peanut protein isolate and cellulose nanocrystals on the properties of Pickering emulsions: Rheological properties and physical stabilities.

The interactions between cellulose nanocrystals and proteins can regulate the interfacial properties of Pickering emulsions, which plays a leading role in the stabilities of Pickering emulsions. In this work, oil-in-water (O/W) Pickering emulsions with different oil-water ratios were prepared using peanut protein isolate modified by cellulose nanocrystals (PPI/CL-CNCs). The distributions of PPI/CL-CNCs at the oil-water interfaces and the microstructures of Pickering emulsions were observed by CLSM and cryo-SEM. The results showed that stable complexes PPI/CL-CNCs formed thick and dense interface layers on the surface of oil droplets. The results of rheological tests clarified that the Pickering emulsions showed an elastic and gel texture, and their gel strength could be enhanced by regulating the oil-water ratios from 3:7 to 7:3. In addition, after one month of storage, the EI of all emulsions remained above 92 % with no obvious phase separation or demulsification. These results suggested that the PPI/CL-CNCs-stabilized Pickering emulsions showed good physical stabilities. The study on the rheological properties and physical stabilities of PPI/CL-CNCs-based Pickering emulsions provided novel insights on developing highly stable Pickering emulsions.