Emulsifying Activity Index Research Articles

Insight into Sequential Extrusion and Cysteine Treatment for Improving Rheological Characteristics and In Vitro Digestibility of Whey Protein Isolate.

The effects of sequential cold extrusion and cysteine (Cys) treatment on the rheological characteristics and in vitro digestibility of whey protein isolate (WPI) were researched in this work. Cold extrusion and Cys treatment increased the apparent viscosity, shear stress, Péclet number, and viscoelasticity of WPI. Furthermore, the emulsifying activity index enhanced in the order of WPI, Cys-treated WPI (Cys-WPI), cold-extruded WPI (CWPI), and extrusion-Cys treated WPI (Cys-CWPI). The emulsion stability index of Cys-CWPI was increased by 29.69% higher than that of WPI. Besides, the α-glucosidase inhibitory rate and xanthine oxidase inhibitory activity in the digests of Cys-CWPI were markedly increased compared with digests of WPI. The synergism of cold extrusion and Cys provides an effective approach for the application of whey protein-based thickeners and emulsifiers; meanwhile, its digestive products may assist in the development of hypoglycemic and uric acid-lowering foods.

Effect of transglutaminase cross-linking on the structure and emulsification performance of heated black bean protein isolate.

Transglutaminase (TGase) is a heat-resistant biocatalyst with strong catalytic activity, which functions effectively under moderate temperature and pH conditions, and is used widely in protein cross-linking and recombination. Transglutaminase cross-linking is a novel and specific modification method for black bean protein isolate (BBPI). This article investigates the effect of transglutaminase cross-linking on the structure and emulsification performance of heated BBPI. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis showed that heated BBPI with TGase had a higher molecular weight than heated BBPI without TGase, and the protein bands widened with increasing enzyme activity, indicating that TGase cross-linking promoted protein molecule aggregation. A high molecular weight polymer can better stabilize the oil-water interface, preventing the emulsion from layering. Fourier transform infrared (FTIR) spectroscopy showed that the α-helix content decreased from 15.64% to 13.75%, and the β-sheet content increased from 48.13% to 54.08%. The decrease in α-helix content and increase in β-sheet content could make the structure more stable and improve the emulsifying properties of heated BBPI. When TGase was 20 U g-1, the protein emulsification activity index (EAI) reached its highest value of 1.87 m2 g-1, and the emulsification stability index (ESI) value was 0.27 min (P < 0.05); these figures were 0.19 m2 g-1, and 0.07 min higher, respectively, than in the sample without added TGase. In summary, transglutaminase cross-linking has a positive effect on the structure and emulsification performance of heated BBPI and can be used as an effective method for BBPI modification. © 2024 Society of Chemical Industry.

Structure and functionality of Pleurotus geesteranus protein isolate as a function of pH.

Edible mushroom proteins hold great potential for food applications, but those extracted using the alkaline extraction-acid precipitation method typically exhibit poor solubility in neutral water, with the structural changes during acid precipitation remaining unclear. In this study, Pleurotus geesteranus protein isolate (PGPI) with high water solubility was prepared with alkaline extraction, followed by dialysis and freeze-drying, and the effects of pH on the structural and functional properties of PGPI were systematically investigated. PGPI was enriched in essential and aromatic amino acids, and the molecular weight of bands in the sodium dodecyl sulfate-polyacrylamide gel electrophoresis profile was mainly distributed below 45kDa. The zeta potential of PGPI changed from +16.84 to 17.58mV when the pH increased from 2 to 9, with a pI of 4.3. At pH 7, PGPI showed a size of 232.7nm. Away from pH 7, the particle size of PGPI increased. When the pH decreased from 7 to 2, PGPI exhibited a lower α-helix structure content and a higher β-sheet content and a gradual decrease in fluorescence intensity. In addition, as the pH approached 4, H0 and the content of SS group increased to a peak. These results indicated that lowering the pH induced the development of more ordered protein structure, which could be the primary reason for the poor water solubility of P. geesteranus protein obtained through alkaline extraction and acid precipitation. Additionally, these structural changes result in alterations to its functional properties, including water-holding capacity, oil-holding capacity, foaming capacity, foaming stability, emulsion activity index, and emulsion stability index.

Comparative study of physicochemical and structural properties of plant proteins hydrolyzed by different

This study used trypsin to hydrolyze soybean protein isolate (SPI), Cyperus esculentus protein (CEP), Wheat gluten protein (WGP), and flaxseed protein (FP) to varying extents, comparing the structure and physicochemical properties of four plant proteins as well as their enzymatic hydrolysates. Results indicate SPI's surface hydrophobicity rises with hydrolysis, whereas CEP's decreases. Additionally, all four plant proteins exhibit improved essential amino acid content and oil-holding capacity as hydrolysis progresses. The CEP with a 20% degree of hydrolysis achieved the optimal oil holding capacity, reaching 10.2 g/g. SPI demonstrated superior foam capacity. As the degree of hydrolysis increased, foam stability varied among the four proteins. The CEP hydrolyzed to 10% exhibited the highest emulsifying activity index, achiving a value of 60 m2/g. Additionally, the emulsifying stability index of CEP hydrolysates significantly improved as the degree of hydrolysis increased. According to the DPPH• assay, both CEP and their enzymatic hydrolysate had the highest free radical scavenging rate. These findings provided a theoretical basis and empirical evidence for the use and adaptation of plant protein hydrolysates as a promising and environmentally sustainable source of plant-derived peptides in food processing reaprocessing.

Encapsulation of resveratrol in nanosheet structured sodium caseinate dialdehyde β-cyclodextrin conjugate with enhanced physicochemical properties

The poor solubility and stability of resveratrol (Res) represent significant obstacles to its utilization and efficacy. Encapsulating in sodium caseinate (NaCas) has also faced issues concerning low encapsulation efficiency and stability. This study presented the synthesis of a novel NaCas and dialdehyde β-cyclodextrin (DA-β-CD) conjugate through the Schiff base reaction using a wet-heating method, which was then utilized to encapsulate resveratrol. Results showed the DA-β-CD was formed in the form of needle-like crystals, whereas the NaCas-DA-β-CD conjugate had a nanosheet structure. The NaCas-DA-β-CD exhibited a substantial increase in surface hydrophobicity, emulsifying activity index, and emulsion stability index. The incorporation of resveratrol into NaCas-DA-β-CD demonstrated a consistent and uniform dispersion at the nanoscale level. It achieved an encapsulation efficiency of 96.8% and exhibited excellent chemical stability, which surpasses those of the NaCas system. Furthermore, the water solubility and antioxidant capacity of resveratrol in NaCas-DA-β-CD exhibited characteristics similar to those in NaCas. The compacted nanosheet structure of the Res-NaCas-DA-β-CD complex, as observed in TEM and SEM, is likely responsible for those enhancements. Hence, the DA-β-CD can serve as an effective polysaccharide for protein modification, while the NaCas-DA-β-CD conjugate can function as an innovative delivery carrier for resveratrol and other hydrophobic bioactives.

Mechanism study on the improvement of egg white emulsifying characteristic by ultrasound synergized citral: Physicochemical properties, molecular flexibility, protein structure

As a natural emulsifier, egg white protein (EWP) has great interfacial characteristics and high security, and has broad development prospects. This study explored the impact of ultrasound synergized citral (CI) treatment on the microstructure, molecular flexibility and emulsifying property of EWP, and predicted the interaction between CI and ovalbumin (the main protein in EWP) through molecular docking. The decrease in free amino content and the growth in molecular weight of EWP suggested that CI and proteins were successfully grafted. The results of physicochemical properties revealed that UCEWP (ultrasound synergized citral-treated EWP) had smaller particle size and larger ζ-potential absolute value, which meant that the stability of UCEWP system was enhanced. From the perspective of interfacial characteristics, UCEWP had lower interfacial tension, which remarkably improved its emulsifying property. The emulsifying activity index (EAI) and emulsifying stability index (ESI) of UCEWP were 1.99 times and 3.19 times higher than that of natural EWP (NEWP). Analysis of Fourier transform infrared spectroscopy (FT-IR) and fluorescence spectroscopy illustrated that the secondary and tertiary structures of UCEWP were more disordered and stretched than those of EWPs. Protein microstructure demonstrated that UCEWP presented loose small particle distribution, and correlation analysis reflected that the improvement of molecular flexibility was positively correlated with the enhancement of emulsifying property. These results elucidated that ultrasound synergized CI treatment is an effective mean to improve the molecular flexibility and emulsifying property of EWP, which provides a valuable reference for further application of EWP.

Synergistic effects of alkaline and heat treatments on structural and functional properties of mung bean protein isolate: improving physicochemical stability of plant‐based emulsions

SummaryPlant‐based meat alternatives often require fat replacers to mimic the texture of traditional products. This study aimed to develop plant‐based emulsion gels using mung bean protein isolate (MBPI) as a potential fat substitute. However, creating these gels via heat setting requires a high protein concentration, which demands modification of the MBPI structure to enhance emulsifying properties. This study investigated synergistic effects of alkaline treatment (0.3 or 3.5% Na2CO3) and heat treatments (40 or 70 °C) on the functional properties of MBPI at high protein levels, for potential application as a plant‐based emulsion. The combined treatments reduced the zeta potential of protein suspensions from −9 to −19 mV and altered the protein conformation to form smaller particles (from 426 to 166 μm) with increased β‐sheet content. These treatments improved dispersibility of 8% MBPI suspension (58 to 86%), emulsifying activity index (6.34–10.89 m2 g−1), and stability coefficient (43 to 96%). Notably, MBPI samples treated with 0.3% Na2CO3 at 40 and 70 °C exhibited excellent emulsifying properties, forming stable monolayers at the oil–water interface, likely due to the increased surface activity of MBPI. Increasing protein concentration to 11% facilitated heat‐set gel formation; however, addition of 3.5%‐Na2CO3 induced premature gelation, limiting its application in emulsions. At 0.3%‐Na2CO3, increasing the protein content from 8% to 11% and the oil content from 10% to 30% further reduced emulsion droplet size, especially for MBPI treated with 0.3% Na2CO3 at 70 °C (MB‐0.3%‐70 °C) from 5.10 to 2.61 μm, likely due to decreased coalescence. This treatment yielded superior MBPI‐stabilised emulsion gels with enhanced penetration, fluid retention, and stability by possibly reducing protein aggregation. These findings demonstrate the potential of MBPI modified by combined addition of 0.3% Na2CO3 and heat treatment, particularly MB‐0.3%‐70 °C, as a promising ingredient for producing plant‐based emulsions.

Thermal stability of γ-PGA modified fish gelatin emulsion.

Emulsions are thermally unstable systems. This research aimed to investigate the thermal stability of fish gelatin (FG) oil-in-water emulsions in the presence of poly-γ-glutamic acid (γ-PGA) as an additive after heat treatment. The study assessed how γ-PGA influences the thermal stability of FG emulsions over time, focusing on their properties, structure, and food application potential. The incorporation of γ-PGA significantly enhanced the thermal stability of FG emulsions, preserving their morphology after heating. Emulsions containing 0.1% γ-PGA showed no significant changes after 24 h at 90 °C, while emulsions without γ-PGA experienced noticeable delamination. Rheological evaluations revealed that the energy storage modulus and loss modulus of FG-γ-PGA emulsions remained consistently higher than those of FG emulsions, regardless of heating duration. Particle size analysis indicated minimal changes for FG-γ-PGA emulsions (413 nm after 24 h) compared to a substantial increase for FG emulsions (1598 nm). After heating, FG-γ-PGA emulsions demonstrated significantly higher emulsifying activity index (EAI) (74 m2 g-1 versus 22.7 m2 g-1) and emulsifying stability index (ESI) (97% versus 76%). Additionally, the texture properties of meat mince formulated with FG-γ-PGA emulsions were comparable to those containing fat, showcasing their potential as a fat replacement. The study concludes that γ-PGA enhances the thermal stability of FG emulsions, maintaining their integrity and improving functional properties under heat treatment. These findings offer valuable insights for the formulation of thermally stable emulsions, presenting promising opportunities for innovative applications in the food industry. © 2024 Society of Chemical Industry.

Spray dried protein concentrates from white button and oyster mushrooms produced by ultrasound-assisted alkaline extraction and isoelectric precipitation.

In the present study, the optimization of ultrasound-assisted alkaline extraction (UAAE) and isoelectric precipitation (IEP) was applied to white button (WBM) and oyster (OYM) mushroom flours to produce functional spray dried mushroom protein concentrates. Solid-to-liquid ratio (5-15% w/v), ultrasound power (0-900 W) and type of acid [HCl or acetic acid (AcOH)] were evaluated for their effect on the extraction and protein yields from mushroom flours submitted to UAAE-IEP protein extraction. Prioritized conditions with maximized protein yield (5% w/v, 900 W, AcOH, for WBM; 5% w/v, 900 W, HCl for OYM) were used to produce spray dried protein concentrates from white button (WBM-PC) and oyster (OYM-PC) mushrooms with high solids recovery (62.3-65.8%). WBM-PC and OYM-PC had high protein content (5.19-5.81 g kg-1), in addition to remarkable foaming capacity (82.5-235.0%) and foam stability (7.0-162.5%), as well as antioxidant phenolics. Highly pH-dependent behavior was observed for solubility (> 90%, at pH 10) and emulsifying properties (emulsification activity index: > 50 m2 g-1, emulsion stability index: > 65%, at pH 10). UAAE-IEP followed by spray drying increased surface hydrophobicity and free sulfhydryl groups by up to 196.5% and 117.5%, respectively, which improved oil holding capacity (359.9-421.0%) and least gelation concentration (6.0-8.0%) of spray dried mushroom protein concentrates. Overall, the present study showed that optimized UAAE-IEP coupled with spray drying is an efficient strategy to produce novel mushroom protein concentrates with enhanced functional attributes for multiple food applications. © 2024 The Author(s). Journal of the Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

Effect of enzymatic hydrolysis and ultrasound pretreatment on allergenicity, functional properties and bioactivity of whey protein isolates

Whey protein isolate (WPI) is an important food ingredient and a major allergen in food. Enzymatic hydrolysis is an important method for WPI modification, but there is limited information on the effect of ultrasound pretreatment on WPI hydrolysates (WPH). The aim of this study was to analyze the effect of enzymatic hydrolysis and ultrasound pretreatment on the allergenicity, functional properties and bioactivity of WPH by multispectroscopy and peptidomics combined with bioinformatics. The results showed that ultrasound pretreatment contributed to the production of WPH with low allergenicity (IgE binding capacity is 55.59%) and good functional properties (emulsifying activity index is 27.02%, foaming characteristic is 50.00%) and bioactivity (total antioxidant capacity is 65.94%). This was attributed to the synergistic hydrolysis of WPI by endopeptidases and exopeptidases, and ultrasound pretreatment that altered the accessibility of WPI to proteases and the peptide profiles and main proteins of WPH, affecting the changes in their spatial and primary structure. This research will advance the application of WPI in hypoallergenic foods.

Structural changes and functional characteristics of common vetch isolate proteins altered by different pH-shifting treatments

To investigate protein structure and functional changes, common vetch protein isolate (CVPI) during pH-shifting were performed. Results showed secondary and tertiary structures of CVPI were improved during these treatments compared with the pH 7.0. Scanning electron microscopy showed the microstructure was changed from lamellar to spherical granular and rod-like structure during pH - shifting. Under 8 pH treatments (pH 2.0, 3.0, 12.0, 2.0 → 7.0, 3.0 → 7.0, 12.0 → 7.0, 11.0 → 9.0 and 11.0 → 7.0), the average particle sizes were smaller and from 82 to 146 nm. Under 8 pH treatments (pH 2.0, 3.0, 11.0, 12.0, 11.0 → 9.0, 11.0 → 7.0,12.0 → 9.0 and 12.0 → 7.0), the protein solubility was higher and from 63 to 86 %. Under 3 pH treatments (pH 2.0, 11.0 and 12.0), the emulsion activity index and emulsion stability index was higher and from 40 to 60 m2/g and from 54 to 97 min. Under 5 pH treatments (pH 2.0, 12.0, 11.0 → 9.0, 12.0 → 9.0 and 12.0 → 7.0), the foaming capacity and foaming stability was higher and from 145 to 185 % and from 67 to 82 %. Therefore, the pH – shifting treatment gave the CVPI improved characteristics in structural and functional properties.

Having their cake and eat it too: Effects of different cations in reduced-salt myofibrillar protein microgel pickering emulsion under high-intensity ultrasound

Health concerns have increased the demand for low-salt emulsified meat products emulsions; however, salt-soluble myofibrillar proteins (MP) are less than optimal emulsifiers under low-salt conditions. In this study, four different cations (Na+, K+, Ca2+, and Mg2+) were added to a Pickering emulsion and high-intensity ultrasound (HIU, 20 kHz, 600 W) was used to determine the quality of the final emulsion. The divalent cation group was found to significantly (P < 0.05) improve the emulsification performance of the emulsion; in particular, the emulsion activity index and emulsion stability index of Mg2+-H group increased to 16.24 ± 1.22 m2/g and 89.66 ± 3.01%, respectively. Measurements of the particle size and zeta potential confirmed that the emulsion particle size of the Mg2+-H group decreased, and the electrostatic repulsion force increased. Based on the surface hydrophobicity and endogenous tryptophan spectra, the particle structure of the MP microgel was determined to be a more stable emulsifier. What's more, the divalent cations promoted the droplets to become evenly dispersed under high-intensity ultrasound. The micrograph confirmed this result: the divalent cation group emulsion was more uniform and stable than the monovalent cation group emulsion. Divalent cations are more suitable than monovalent cations for improving the quality of reduced-salt Pickering emulsions.

Modulating the techno-functional properties of quinoa (Chenopodium quinoa Wild) protein concentrate using high-pressure technologies and their impact on in vitro digestibility: A comparative study

High hydrostatic pressure (HHP; 200–600 MPa at 24 °C for 20 min) and dynamic high pressure (DHP; 50–180 MPa) were applied to modulate the techno-functional properties of quinoa protein concentrate (QPC) produced from non-defatted flour using a lab-scale extraction. QPC's unique composition, with 74.6 % protein and significant levels of unsaturated fatty acids, influenced the effects of HHP and DHP. HHP significantly (P < 0.05) enhanced hydration properties, peaking at 400 and 500 MPa (on average 4.34 g/g), while DHP reduced the oil absorption capacity from 2.5 to 1.8 g/g. Both processing techniques decreased QPC protein solubility. This reduction corresponded to decreased foaming capacity and emulsifying properties in HHP-processed QPC. DHP increased emulsifying activity and stability indices, with optimized improvements at 100 MPa of 39.4 and 414.4 %, respectively. These modifications in QPC's properties occurred without noticeable loss in in vitro protein digestibility (IVPDaverage = 86.1 %). The findings support the potential of high-pressure technologies to uniquely modulate different techno-functional properties of QPC, produced from non-defatted flour, while maintaining high digestibility, thereby offering greater versatility in its use. Industrial relevanceQuinoa is a strategic choice for diversifying plant protein sources, with the use of non-defatted flour in QPC production offering new insights into its composition and properties, reducing both costs and environmental impact. In this study, HHP and DHP, recognized as “green” physical processing technologies, demonstrated advantageous potential to develop innovative quinoa protein ingredients with added value and clean-label appeal, while maintaining their high nutritional value. The distinctive effects of high-pressure technologies and varying pressure levels on modulating QPC's techno-functional properties underscore the creation of multifunctional QPC and the optimization of key properties, addressing the urgent demands of the plant-based food segment.

Modification of pepper seed protein isolate to improve its functional characteristic by high hydrostatic pressure

Pepper seed protein isolate (PSPI) is a valuable plant-based protein source, yet the impact of processing methods such as high hydrostatic pressure (HHP) on its properties remains unclear. The impact of HHP on the structural and functional properties of PSPI at pH 7 and pH 9 was evaluated. Structural changes in PSPI were analyzed using spectral techniques, revealing significant alterations in the secondary and tertiary structures induced by HHP treatment. HHP treatment caused the unfolding of the PSPI structure, leading to the exposure of previously hidden chromophores and hydrophobic groups. The treatment also led to changes in free sulfhydryl groups and increased average particle size suggesting the formation of macromolecular polymers or insoluble aggregates. Consequently, the water-holding capacity, oil-holding capacity, foaming characteristics, and emulsifying activity index of the modified PSPI were significantly enhanced both at pH 7 and pH 9, with maximum improvements of 121.98 %, 157.29 %, 100.00 %, and 265.78 %, respectively. In conclusion, HHP is a promising strategy for enhancing the physicochemical properties of PSPI for various applications.

Hofmeister ion effects induced by different acidifiers and alkalizers improve the techno-functional properties of complex rapeseed protein during pH-driven self-assembly

pH-driven method is an effective strategy to prepare complex protein. This study provides guidance on how to select acidifiers and alkalizers from view of Hofmeister ion effects. Cations and anions regulated the molecular structure (particle size, surface charge, protein folding/unfolding, structural orderliness) of complex rapeseed proteins (CRPs) mainly via electrostatic and hydrogen bond. No evident changes were found in the molecular weight distribution, but their distribution on oil/air-water interface varied greatly. Various techno-functional properties of CRPs were synergistically improved: Citrate3− and Na+ increased the emulsifying activity index of CRPs from 80 to 102.21 m2/g; Citrate3−, K+ and Na+ made the foaming stability of CRPs close to 80 % after 60 min of storage. Moreover, the oil/water-holding and gel properties of CRPs were regulated effectively. These findings demonstrate the key role of Hofmeister ion effects in improving CRPs properties, contributing to develop, select, and apply novel acidifiers and alkalizers during pH-driven treatment.

Noncovalent interaction between proanthocyanidins and soy protein isolate fibers: Structure, functionality and interaction mechanism

This study focused on the addition of different concentrations of proanthocyanidins (OPC) to form noncovalent complexes with soy protein isolate fibers (SPIF). To investigate the effects of polyphenols on the structural and functional properties of protein fibers and to elucidate the mechanism of their interaction. The addition of OPC unfolded the internal structure of the proteins, exposing the hydrophobic groups and reducing the β-sheet structure of SPIF, forming the SPIF-OPC complexes. And the binding of the two would be close to saturation, at the final concentration of added OPC was 0.5 or 1 mg/mL. Multiple spectroscopy and isothermal titration calorimetry analyses indicated that static quenching was the mechanism of fluorescence quenching of SPIF by OPC. The two spontaneously combined through hydrogen bonding and hydrophobic interactions. Transmission electron microscopy observations of the microscopic morphology also indicated that the addition of OPC altered the original long, semi-flexible fibers structure of SPIF. The fibers gradually showed a large number of branches and became short and curved. When the final concentration of added OPC was 4 mg/mL, the emulsifying activity index of SPIF increased by 78.40% and the foaming capacity of SPIF increased by 37.10%. The interaction mechanism of different concentrations of OPC with SPIF will be comprehensively understood from this study, thus expanding its application in food, medicine, cosmetics, and other fields.

How does high hydrostatic pressure treatment improve the esterification of quinoa (Chenopodium quinoa Willd.) starch?

High hydrostatic pressure (HHP) treatment was combined with octenyl succinic anhydride (OSA) modification of quinoa starch (QS) to improve esterification efficiency. The modified QS was used as a stabilizer to prepare a Pickering emulsion. The results showed that the HHP treatment disrupted the morphology and crystalline structure of QS, exposed numerous hydrophilic hydroxyl groups, and added esterification reaction sites. The degree of substitution (DS) and esterification efficiency (RE) of OSA-HHP-QS were significantly (p < 0.05) increased compared with OSA-QS. In addition, the short-range ordering, relative crystallinity, and thermal stability of OSA-HHP-QS decreased with increasing treatment pressure. Except for OSA-HHP200-QS, the starch granules treated at 200 MPa were annealed, resulting in molecular recrystallization. The Contact angle, emulsion stability index (ESI), and emulsion activity index (EAI) indicated that the emulsions stabilized with OSA-HHP-QS were highly stable. Therefore, HHP can be used as a novel technology to assist OSA modified starches in stabilizing Pickering emulsions.

Effects of different oxidation methods on the functional properties and gel characteristics of hazelnut proteins

SummaryThis study aimed to investigate the effects of different oxidation modes on the functional and gel properties of hazelnut proteins. The solubility of hazelnut protein showed a small trend when the oxidation level was low, and it decreased significantly with the increase in concentration. The maximum value of water‐holding capacity (WHC), emulsifying activity index (EAI), and emulsion stability index (ESI) was 343.33%, 56.00 m2 g−1, and 75.85 min at AAPH concentration of 1.0 mmol L−1, respectively. The functional properties of hazelnut proteins, except oil‐holding capacity (OHC), gradually reduced with the increase in malondialdehyde (MDA) concentration. H2O2 modified improved OHC, foaming capacity, foam stability, and EAI of hazelnut proteins, whereas WHC and ESI gradually decreased. The results of the secondary structure of hazelnut protein gels indicated a high ratio of α‐helix and β‐fold of the gels. Also, the increase in oxidation led to an increase in the gels' voids. Also, oxidation led to a rough and loose network structure of hazelnut protein gels. These results suggested that peroxyl radical, hydroxyl radical, and MDA produced during lipid peroxidation affected the interfacial properties of hazelnut protein and disrupted the formation of hazelnut protein gel, thus affecting the quality of hazelnut protein.

Effects of papain hydrolysate of Pseudosciaena crocea roe on the physical and oxidative stability of water-in-oil emulsions

This study investigates the effects of hydrolysates from Pseudosciaena crocea roe on the physical and oxidative stability of oil-in-water emulsions, emphasizing the structure-activity relationship between peptide structure and emulsifying properties. The results showed that, compared to other proteases, hydrolysates prepared with papain (PCRHs) at moderate degrees of hydrolysis (DH 4.68% and 6.8%) exhibited superior emulsifying activity index (EAI) and emulsifying stability index (ESI). PCRHs with DH of 4.68%, 6.8% formed smaller particle sizes (89.8 ± 3.52 nm, 112 ± 2.65 nm) and more stable emulsions. EAI and ESI of PCRHs were significantly negatively correlated with emulsion particle size and significantly positively correlated with surface hydrophobicity, amino acid composition, relative molecular mass, random coil content and total sulfhydryl groups. Additionally, although PCRHs with DH of 4.68% produced smaller and more stable emulsion particles, PCRHs with DH of 6.8% significantly inhibited primary and secondary lipid oxidation products formation. Correlation analysis revealed that emulsions with smaller particle sizes exhibited poorer oxidative stability, and secondary volatile oxidation products better reflected the oxidative stability of emulsions. Therefore, hydrolysates from Pseudosciaena crocea roe protein with moderate hydrolysis, particularly PCRHs with DH of 6.8%, demonstrate potential as natural emulsifiers to maintain the physical and oxidative stability of oil-in-water emulsions.

Emulsion Stability and Rheological Properties of Emulsions Prepared with Ozonized Hazelnut Oil

In this study, physical and rheological characteristics of the emulsion stabilized with whey protein isolate (WPI) at a concentration of 0.25% (w/w) and containing ozone applicated hazelnut oil (OHO) were studied. The hazelnut oil was subjected to ozone gas exposure for durations of 1, 5, 30, 60, 180, and 360 min. The emulsions made with both control (HO) and OHO were analysed to assess emulsion properties. It was observed that as the duration of ozone application increased, the emulsion activity index (EAI) experienced a decrease. Specifically, ozone applications of 30, 60, and 180 min significantly reduced emulsion stability index (ESI). The creaming ratio of emulsions formulated with OHO for durations of 1, 5, 30, 60, and 180 min were found to be 23%, 20%, 18%, 16%, and 44%, respectively. Optical microscopy revealed that significant flocculated droplet formed in emulsions including OHO. The longer time the ozone application resulted that the emulsions exhibited more solid-like behaviour. Furthermore, differential scanning calorimeter (DSC) was utilized to assess the changes in the melting and cooling profiles of hazelnut oil after being applicated with ozone. An increase in ozone application duration led to the melting peaks broadening and shifting towards lower temperatures. Also, ozone application caused that the sharp exothermic crystallization shifted towards lower temperatures and become broader and less pronounced as the duration of the application increased.