Whey Protein Isolate Research Articles

Storage stability and antioxidant activity of astaxanthin and beta-carotene as affected by the architecture of O/W emulsions of milk proteins

Astaxanthin and β-carotene are among the potential anti-oxidant carotenoids with strong health promoting features. However, their sensitivity to light, heat and mechanical forces limit their application in food processing and storage conditions. The design of food matrix system, such as emulsions, that could prevent them from exposure to environmental factors will be utmost importance to slow down their degradation. In this study, O/W emulsion systems containing sunflower oil were prepared by applying ultrasound treatment and using different stabilizers (i.e. whey protein isolate (WPI) and sodium caseinate; NaCAS), co-surfactants (pectin and lecithin) while their performance against physical and chemical stability were investigated. The WPI– lecithin system produced emulsion droplets with Average diameter in the range of 560–2900 nm with a zeta-potential in the range of (−31) – (−34) mV, whereas the NaCAS – lecithin systems produced emulsion droplets with average diameter in the range of 230–240 nm and zeta potential of (−44) – (−48) mV. These values have a direct effect on the physical stability and chemical stability of the carotenoids in the emulsions. Astaxanthin was found to be more sensitive than β-carotene to ultrasound processing conditions. The designed emulsion systems slowed down the degradation of the carotenoids and maintained their DPPH scavenging properties during storage with astaxanthin loaded emulsions exhibiting better DPPH activity than β-carotene loaded emulsions.

Characteristics of pomegranate (Punica granatum L.) peel polyphenols encapsulated with whey protein isolate and β-cyclodextrin by spray-drying

Pomegranate peel polyphenols (PPPs) are recognized as promising food additives due to their diverse bioactivities; however, their application is limited by poor stability. To address this critical issue, three types of PPPs microcapsules were prepared using β-cyclodextrin (CD), whey protein isolate (WPI), and a composite material of CD-WPI through ultrasound treatment (US). Results revealed that ultrasound treatment can enhance the PPPs-wall material interaction, as evidenced by MD simulations. The encapsulation efficiency of CD-WPI-PPPs was 93.73 %, which was significantly higher than that of CD-PPPs and WPI-PPPs (p < 0.05). The degradation rate constant of CD-WPI-PPPs was reduced by 95.83 %, and its t1/2 was extended by 23-fold compared to that of unencapsulated PPPs. Furthermore, CD-WPI-PPPs exhibited greater DPPH scavenging activity and inhibited polyphenol release during oral and gastric digestion while promoting release during intestinal digestion. These outcomes were attributed to enhanced integrity and interactions between PPPs and composite materials in the microcapsules formed through ultrasound treatment, as supported by SEM images and FT-IR spectra. Consequently, the application of US in the preparation of PPPs microcapsules presents a promising strategy for developing natural nutrient additives for food applications, thereby enhancing the functional properties of food products.

Impact of microstructure of whey protein gels on in vitro gastric protein digestion is sustained after oral structural breakdown by mastication

Gastric protein digestion can be influenced by food micro- and macrostructure. Understanding the interplay between microstructure and macrostructural breakdown during oral processing is crucial to enhance the nutritional value of protein-rich foods. This study compared the in vitro gastric protein digestion of whey protein gels differing in microstructure before and after mastication. Whey protein isolate was mixed with κ-carrageenan to obtain heat-induced gels differing in microstructure (homogeneous, coarse stranded, protein continuous, bi-continuous). Gel boli were collected from 14 participants. The number, size and total surface area of bolus fragments were determined. In vitro gastric protein digestion was quantified following the INFOGEST 2.0 protocol with minor modifications. Before mastication, coarse stranded gels showed the highest digestion rate (1.07 mmol L−1∙g dry matter−1/h), while homogeneous, protein continuous and bi-continuous gels showed lower and similar digestion rates (0.82–0.87 mmol L−1∙g dry matter−1/h). After mastication, the total surface area of coarse stranded gels increased 7.9-fold leading to a 1.9-fold increase in digestion rate. In contrast, a 3.4-fold increase in total surface area of bi-continuous gels caused a 2.8-fold increase in digestion rate. The total surface area of homogeneous and protein continuous gels increased 3.1- to 3.6-fold upon mastication resulting in a 1.7- to 1.9-fold increase in digestion rate. The increase in protein hydrolysis did not correlate with the degree of structural breakdown after mastication across gels differing in microstructure. We conclude that the impact of microstructure of whey protein gels on in vitro gastric protein digestion is sustained after oral structural breakdown by mastication.

Amphiphilic colloidal particles/Ca2+ reinforced edible agar nanocomposite film by multiple cross-linking/microphase separation strategies

The agar (AG) film exhibited poor mechanical and water-resistant properties which limited its application for food packaging. The structural modification of AG nanocomposite film greatly impacts their macroscopic properties. In this paper, edible AG nanocomposite films were achieved by incorporating colloidal particles based on conjugates of whey protein isolate (WPI) and alginate oligosaccharides (AOS) as the nanofiller to obtain the micro-phase separation structure and the multiple cross-linking network with the synergistic interactions of the Ca2+ crosslinking. Firstly, WPI-AOS colloidal particles were synthesized through the Wet-heating Maillard reaction. Good compatibility between WPI-AOS colloidal particles and AG was exhibited, resulting in improved mechanical and water-resistant properties of AG composite films. Compared to pure AG film, the tensile strength (TS) of the agar composite film with 10% WPI-AOS colloidal particles increased significantly to 81.87 MPa from 24.02 MPa, and the elongation at break (EAB) also improved to 46.25% from 18.65%. The moisture content (MC), water solubility (WS), and water vapor permeability (WVP) of the AG composite film decreased by 33.1%, 18.0%, and 22.4% respectively. In addition, the multiple cross-linking network hindered the relative sliding between the AG molecular chain, which resulted in improved thermal stability of the composite film. Using soft colloidal particles as nanofillers to fabricate edible films for improving their properties is an effective and promising strategy.

Exploration of binding mechanism of whey protein isolate and proanthocyanidin: Spectroscopic analysis and molecular dynamics simulation

The non-covalent whey protein isolate-proanthocyanidin (WPI-PC) complex was constructed and possessed superior anti-muscle attenuation activity in our previous study. While the non-covalent binding mechanism of WPI and PC remains unclear. The interaction mechanism of whey protein isolate (WPI) and proanthocyanidin (PC) was explored using multispectral analysis and molecular dynamics (MD) simulation. The results indicated that the non-covalent binding of PC and WPI led to fluorescence quenching, causing the conformational changes and microenvironment changes of WPI. The surface hydrophobicity of WPI-PC complex was reduced by 42.36 % compared with WPI (P < 0.05). The hydrogen bond and hydrophobic interaction were involved in the interaction between WPI and PC, and hydrogen bond played a dominant role. The WPI-PC complex was irregular and showed a smaller sheet structure. The PC and WPI remained a stable binding mainly through 15 key residues, especially the energy contribution of LEU 39. Additionally, the flexibility and fluctuation of individual amino acid residues in WPI were altered after binding to PC. It is hoped that this study could provide theoretical basis for the application of WPI and PC in functional foods.

Pickering Foam Stabilized by Diacylglycerol-Based Solid Lipid Nanoparticles: Effect of Protein Modification.

Pickering foams have great potential for applications in aerated foods, but their foaming ability and physical stability are still far from satisfactory. Herein, solid lipid particles (SLNs) were fabricated by using diacylglycerol of varying acyl chain lengths with modification by a protein. The SLNs showed different crystal polymorphisms and air-water interfacial activity. C14-DAG SLN with a contact angle ∼ 79° formed aqueous foam with supreme stability and high plasticity. Whey protein isolate and sodium caseinate (0.1 wt %) considerably enhanced the foamability and interfacial activity of SLNs and promoted the packing of particles at the bubble surface. However, high protein concentration caused foam destruction due to the competitive adsorption effect. β-sheet increased in protein after adsorption and changed the polymorphism and thermodynamic properties of SLN. The foam collapsing behaviors varied in the presence of protein. The results gave insights into fabricating ultrastable aqueous foams by using high-melting DAG particles. The obtained foams demonstrated good temperature sensitivity and plasticity, which showed promising application prospects in the food and cosmetic fields.

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.

Whey protein isolate-tamarind seed gum complexes stabilized dysphagia friendly high internal phase emulsions: The effects of pH conditions and mass ratios

Dysphagia is a common malfunction affecting a large population worldwide, yet the range of food available to the patients is limited. The objective of this study was to utilize a complex of whey protein isolate (WPI) and tamarind seed gum (TG) as novel emulsifiers to stabilize HIPEs, and further explore WPI-TG-based HIPEs' potential as dysphagia-friendly foods for special medical purposes (FSMP). The results indicated that WPI-TG forms complexes through hydrogen bonding and electrostatic interactions (pH 3 and 4). Additionally, TG induced changes in the secondary and tertiary structures of WPI. The particle size of HIPEs prepared from WPI-TG complexes was found to be reduced. Meanwhile, with the decrease in pH from 7 to 3, the variation in complexes ζ-potential led to an initial increase followed by a subsequent drop in the particle size of HIPEs. The rheological results indicated that WPI-TG-based HIPEs exhibit low-risk swallow characteristics, including shear thinning, high storage modulus, and good recovery ability. Further analysis using the IDDSI testing demonstrated that WPI-TG-based HIPEs under pH 3 and 4 can potentially be dysphagia-friendly FSMPs. After undergoing thermal treatment or long-term storage, WPI-TG-based HIPEs at pH 3 and 4 consistently maintained compliance with the IDDSI testing. These findings provided valuable insights for the future utilization of HIPEs in developing dysphagia-friendly FSMPs.

Fabrication and characterization of whey protein isolate-tryptophan nanoparticles by pH-shifting combined with heat treatment

L-Tryptophan (Trp) is an essential amino acid with numerous health benefits. However, incorporating Trp into food products is limited due to its pronounced bitter taste. Encapsulating Trp in nanoparticles by using other natural biopolymers is a potential strategy to mask the bitter taste of Trp in the final products. Whey protein isolate (WPI), composed of alpha-lactalbumin (α-LA), bovine serum albumin (BSA), and beta-lactoglobulin (β-LG), has played a crucial role in delivering bioactive compounds. In order to incorporate Trp within WPI, the present study used a combination of pH-shifting andthermal treatment to fabricatewhey protein isolate-tryptophan nanoparticles (WPI-Trp-NPs). During the pH-shifting technique, WPI unfolds at high pH, such as pH 11, and the dissociated WPI molecules are refolded when pH is shifted back to neutral, creating particles with uniform dispersion and encapsulating smaller particles surrounding them in solution. Further, the well-distributed nanoparticles formed by pH-shifting might encourage the formation of more uniform nanoparticles during subsequent thermal treatment. TheWPI-Trp particles have an average particle size of 110.1 nm and a low average PDI of 0.20. Fluorescence spectroscopy confirmed the encapsulation of Trp by WPI, which shows higher fluorescence when the Trp is encapsulated by the WPI. Surface hydrophobicity, circular dichroism, particle size, free sulfhydryl, and antioxidant activity were used to characterize the WPI-Trp-NPs. WPI-Trp-NPs formed by pH-shifting combined with heating showed a higher surface hydrophobicity and free sulfhydryl content than the untreated WPI-Trp mixture. The conversion of α-helix into random coil in the WPI secondary structure indicated a more disordered structure of the modified whey protein. Molecular docking results indicate the interactions between Trp and WPI, including alpha-lactalbumin (α-LA), bovine serum albumin, and beta-lactoglobulin (β-LG), were mainly driven by hydrophobic interactions and hydrogen bonding. The binding affinity between Trp and these proteins was ranked as α-LA>BSA>β-LG. The combination of pH-shifting and heating improved the functionalityof WPI and was an effective way to fabricate WPI-Trp nanoparticles.

Dynamic high-pressure microfluidization assisted with galactooligosaccharide-modified whey protein isolate: Investigating its effect on relieving intestinal barrier damage

The study aimed to investigating the mechanisms of relieved intestinal barrier damage by dynamic high-pressure microfluidization assisted with galactooligosaccharide- glycated whey protein isolate. The modifications changed the multi-structure, and the modified whey protein isolate could promote the proliferation of IEC-6 cells and contributed to the restoration of LPS-induced occludin damage in IEC-6 cells. Also, it could repair cyclophosphamide-induced ileal villus rupture and crypt destruction in BALB/c mice, significantly altered the abundance of dominant bacteria, which were associated with propionic acid, butyric acid, isovaleric acid, and valeric acid. Ileum transcriptomics revealed that the modified whey protein isolate significantly regulate of the levels of Cstad, Cyp11a1, and Hs6st2 genes, relating to the increase of propionic acid, isovaleric acid, and valeric acid. In conclusion, galactooligosaccharide- modified whey protein isolate could regulate the level of Cstad, Cyp11a1 and Hs6st2 genes by altering the gut microbial structure and the level of SCFAs, thereby repairing the intestinal barrier.

Mechanistic insights into the interaction of Lycium barbarum polysaccharide with whey protein isolate: Functional and structural characterization

Protein-polysaccharide interactions are crucial for food system structure and stability. This study investigates the interaction of Lycium barbarum polysaccharide (LBP) at 0–2.00 % concentrations with whey protein isolate (WPI), focusing on functionality and structural changes. LBP covalently grafted onto WPI, as confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), forming WPI-LBP complexes with a maximum degree of grafting (DG) of 44.58 % at 2.00 % LBP. This grafting reduced WPI's surface hydrophobicity (H0) and improved solubility, emulsifying properties, and digestibility under certain conditions, with optimal antioxidant activity at 1.00 % LBP. Multispectral analysis and microscopy showed LBP grafting alters WPI's secondary, tertiary, crystalline, and micro/nanostructures. The comprehensive analysis indicates that the interaction between LBP and WPI involves covalent bonding, hydrogen bonding, hydrophobic interactions, and electrostatic forces, as supported by zeta potential and chemical forces results. These findings suggest LBP-protein complexes as promising food materials for enhancing functionality and stability in the food industry.

Proteins make tea polyphenol EGCG not always develop satisfactory α-glucosidase inhibition: The influences of three proteins on α-glucosidase inhibitory activity of EGCG

Tea polyphenol epigallocatechin-3-gallate (EGCG) has been previously explored as an effective inhibitor of carbohydrate hydrolyzing α-glucosidase for regulating postprandial blood glucose level. Proteins act as one common dietary component, the influence of which on α-glucosidase inhibition of EGCG remains unknown. In this study, bovine serum albumin (BSA) and isolated whey protein (IWP) were found to significantly weaken the competitive inhibitory activity of EGCG against α-glucosidase by the effect order of BSA > IWP, while egg albumin (EA) hardly influenced the enzyme inhibition. Through the analyses of kinetics, spectroscopy, thermodynamics and simulated docking, a protein-EGCG-enzyme ternary complex was suggested to generate in the interaction system, in which there existed competition between proteins (BSA and IWP) and α-glucosidase regarding formation of hydrogen bondings with polyphenolic groups (especially galloyl moiety). This weakened the EGCG-enzyme binding interactions at α-glucosidase active site, and thus reduced the enzyme inhibition in vitro and in vivo. However, there existed a co-existing relationship between proteins and α-glucosidase regarding π-stackings of EGCG benzene ring with aromatic residues of both macromolecules, which remained the fluorescence quenching ability of EGCG against the enzyme. Conclusively, dietary proteins should be considered as a potential influence factor when developing natural products as inhibitors of carbohydrate hydrolyzing enzymes.

Heat-induced interactions between microfluidized hemp protein particles and caseins or whey proteins

The rising demand for sustainable proteins leads to increased interest in plant proteins like hemp protein (HP). However, commercial HP's poor functionality, including heat aggregation, limit its use. This study explored the heat-induced interactions of hemp protein particles (HPPs) with milk proteins, specifically whey proteins and caseins. Using various analysis techniques—static light scattering, TEM, SDS electrophoresis, surface hydrophobicity, and free sulfhydryl content—results showed that co-heating HPPs with whey protein isolate (WPI) or sodium caseinate (NaCN) at 95 °C for 20 min reduced HPPs aggregation. HPPs/WPI particles had a d4,3 of ∼3.8 μm, while HPPs/NaCN were ∼1.9 μm, compared to ∼27.5 μm for HPPs alone. SDS-PAGE indicated that whey proteins irreversibly bound to HPPs, through disulfide bonds, whereas casein bound reversibly, possibly involving the chaperone-like property of casein. This study proposes possible mechanisms by which HPPs interact with milk proteins and impact protein aggregation. This may provide opportunities for developing hybrid protein microparticles.

Improved viability of probiotics by co-encapsulation of wheat germ oil under storage and gastrointestinal conditions: Effects of drying methods and wall composition

To improve the viability of probiotics during food storage and gastrointestinal digestion, this study developed solid microcapsules co-loaded with probiotics and wheat germ oil using W1/O/W2 emulsion pre-encapsulation, followed by spray drying (SD), freeze drying (FD) and spray freeze drying (SFD), respectively. The effects of drying methods and wall materials on the microstructure, physicochemical properties, storage stability, and gastrointestinal tolerability were highlighted. Firstly, all samples showed high encapsulation efficiency for probiotics (86%–99.2%) and wheat germ oil (72%–85%), low moisture content (2.8%–5.3%) and hygroscopicity (6.3%–11.6%), and wall materials exhibited structural stability during the drying process. The results of viable cell counts indicated that SFD caused more damage to bacterial cells than the other two drying methods, as evidenced by the total death of encapsulated probiotics within 90 days. In contrast, SD and FD encapsulated probiotics remained at 8.8–9.9 log CFU/g after 150 days of storage at 4 °C and 25 °C. Furthermore, the viability of probiotics in the co-encapsulated and pectin-added microcapsules was significantly enhanced in storage stability and simulated gastrointestinal digestion tests. Based on the above results, it was suggested that the co-encapsulation strategy of combining the W1/O/W2 structure and SD or FD to prepare microencapsulated powders can obtain probiotic products with high activity and high stability. Meanwhile, composite wall material (whey protein isolate and pectin) could enhance probiotics' protective effect and colonic targeted release behavior. In conclusion, the current research provides a valuable reference for the application of probiotics and functional oils in the food industry.

Enhancing the water dispersibility and intestinal targeting of pterostilbene using tannic acid-whey protein conjugates

In this study, three types of whey protein isolate (WPI)-tannic acid (TA) covalent conjugates (WPI-TA) were synthesized via alkaline treatment, free radical-induced method, and laccase induction. These conjugates were subsequently utilized in the antisolvent precipitation method to encapsulate pterostilbene (Pte). The structural and functional properties of these conjugates as carriers for intestinal-targeted Pte delivery were thoroughly evaluated. SDS-PAGE, total phenolic content measurement, grafting efficiency, and FT-IR analysis confirmed the successful formation of three distinct covalent conjugates. Among them, the laccase-induced WPI-TA conjugates exhibited the highest TA grafting efficiency. The particle size of this conjugate was measured at 115.25 nm with a PDI of 0.31. Upon encapsulation of Pte, this conjugate exhibited superior thermal stability, enhanced antioxidant properties, and sustained release within the gastrointestinal tract. The water solubility of Pte in these nanoparticles was found to be 361.19 times higher than that of free Pte, presenting a promising strategy for targeted intestinal delivery of Pte.

Influence of pH on thermal stability of mixed dairy and plant protein systems

SummaryThe growing global population has increased the protein needs and the combination of animal with plant proteins can be an effective strategy to meet future protein demand. This study aimed to investigate the impact of pH between 6.2 and 7.0 on the thermal stability of a 1:1 mixture of chickpea protein concentrate (CPC) and whey protein isolate (WPI), and their respective control. After heat treatment, CPC:WPI mixture showed an increase in viscosity (from 20.5 mPa.s at pH 7.0 to 110.8 mPa.s at pH 6.2, respectively), and particle size (from 5.7 to 56.5 μm at pH 7.0 and 6.2, respectively). The physical stability of the heat‐treated CPC:WPI mixture decreased, as the sediment increased from 3.3 mm at pH 7.0 to 7.8 mm at pH 6.2. This study highlighted the enhanced thermal stability of CPC:WPI at pHs closer to neutrality and offers valuable insights for the formulation of innovative plant protein‐enriched food.

Effects of mixing ratio on physicochemical, structural properties and application in lycopene-loaded emulsions of blends of whey protein and pea protein

Physicochemical, structural properties and application in lycopene-loaded emulsions of blends of whey protein isolate (WPI) and pea protein isolate (PPI) at varying mass ratios (100/0, 75/25, 50/50, 25/75, 0/100) were investigated. Data indicated that the mass ratios affected the physical, chemical and storage stability of the emulsion by influencing the particle size, zeta-potential, surface hydrophobicity, free sulfhydryl content, and secondary structure of the blends. Particularly, emulsion with a mixing ratio of 75/25 exhibited superior physical stability against salt concentrations (200 and 500 mM), better chemical stability against UV light and heat, and maintained stability over a 30-day storage period. Emulsions stabilized by blends of different ratios exhibited similar digestion behavior, with no significant differences observed in lycopene's transformation stability and bio-accessibility. Data indicated that substitution of whey protein by pea protein is effective in term of emulsifier application and replacement ratio is an important factor need to be considered.

Development of Oleogel-in-Water High Internal Phase Emulsions with Improved Physicochemical Stability and Their Application in Mayonnaise.

Egg-free mayonnaise is receiving greater attention due to its potential health benefits. This study used whey protein isolate (WPI) as an emulsifier to develop high internal phase emulsions (HIPEs) based on beeswax (BW) oleogels through a simple one-step method. The effects of WPI, NaCl and sucrose on the physicochemical properties of HIPEs were investigated. A novel simulated mayonnaise was then prepared and characterized. Microstructural observation revealed that WPI enveloped oil droplets at the interface, forming a typical O/W emulsion. Increase in WPI content led to significantly enhanced stability of HIPEs, and HIPEs with 5% WPI had the smallest particle size (11.9 ± 0.18 μm). With the increase in NaCl concentration, particle size was increased and ζ-potential was decreased. Higher sucrose content led to reduced particle size and ζ-potential, and slightly improved stability. Rheological tests indicated solid-like properties and shear-thinning behaviors in all HIPEs. The addition of WPI and sucrose improved the structures and viscosity of HIPEs. Simulated mayonnaises (WE-0.3%, WE-1% and YE) were then prepared based on the above HIPEs. Compared to commercial mayonnaises, the mayonnaises based on HIPEs exhibited higher viscoelastic modulus and similar tribological characteristics, indicating the potential application feasibility of oleogel-based HIPEs in mayonnaise. These findings provided insights into the development of novel and healthier mayonnaise alternatives.

Going back to the basics: the use of cricket powder as a protein supplement in artificial ant diets

The ability to keep stable, healthy colonies in laboratory settings is fundamental for conducting research on ants and particularly important for developing management tools for pest species. An important component for successful ant rearing is a suitable diet and a number of diets for feeding ants have been developed. Calcium caseinate as a protein supplement has been a widely used ingredient in ant diets, but it has become difficult to obtain. Therefore, there is a need to find an alternative protein supplement for rearing ants in captivity. Using the ant Nylanderia fulva as a model, the suitability of four alternative diets was tested against a calcium caseinate containing diet: (1) whey protein isolate fortified with calcium, (2) whey protein isolate, (3) sodium caseinate, and (4) cricket powder. We tested the performance of colony fragments fed on diets by comparing worker and queen mortality, as well as brood production for 6 weeks. Diet containing cricket powder performed better than all other diets, reflected by lower worker mortality and the addition of new workers and brood to the colony fragment, resulting in colony growth. Considering recent developments in the production of cricket powder making it a low cost and readily accessible ingredient, it should prove an effective protein supplement for rearing ants in captivity for other species.

Physicochemical Properties, Functionalities, and Antioxidant Activity of Protein Extracts from New Zealand Wild Sea Cucumbers (Australostichopus mollis).

This study investigated the physicochemical properties, functionalities, and antioxidant capacities of protein extracts from wild sea cucumber Australostichopus mollis collected from four distinct locations in New Zealand. Protein was extracted from sea cucumber body walls using trypsin enzymatic extraction, followed by cold acetone precipitation. The amino acid analysis revealed high glycine (189.08 mg/g), glutamic acid (119.45 mg/g), and aspartic acid (91.91 mg/g) concentrations in all samples. The essential amino acid indexes of the protein extracts (62.96, average) were higher than the WHO/FAO standard references, indicating the excellent protein quality of A. mollis. Furthermore, protein extracts from A. mollis demonstrated superior emulsifying activity (202.3-349.5 m2/g average) compared to commercial soy and whey protein isolates under all tested pH conditions, and enhanced foaming capacity (109.9-126.4%) and stability (52.7-72%) in neutral and acidic conditions. The extracts also exhibited good solubility, exceeding 70% across pH 3-11. Antioxidant capacities (ABTS and DPPH free radical scavenging activity and ferric reducing antioxidant power) were identified in A. mollis protein extracts for the first time, with clear variations observed among different locations. These findings elucidate the advantageous functional properties of protein extracts from wild New Zealand A. mollis and highlight their potential application as high-quality antioxidant food ingredients.