Food Hydrocolloids最新文献

{"title":"Role of globulins and albumins in oil-water interface and emulsion stabilization properties of pulse proteins","authors":"Penghui Shen ,&nbsp;Fee Twilt ,&nbsp;Raazia Nazir ,&nbsp;Jinfeng Peng ,&nbsp;Jasper Landman ,&nbsp;Leonard M.C. Sagis","doi":"10.1016/j.foodhyd.2025.111463","DOIUrl":"10.1016/j.foodhyd.2025.111463","url":null,"abstract":"<div><div>Pulse protein extracts have received considerable attention in food applications, for instance, as emulsifiers. These extracts are complex protein mixtures consisting primarily of globulins and albumins, but how these individual protein fractions affect the emulsifying properties is still poorly understood. In this study, we separated globulins and albumins from lentil, faba bean and chickpea, and systematically investigated their role in the stabilization of oil-water interfaces and emulsions. We identified key molecular and interfacial parameters of these pulse proteins (including the whole protein mixtures) which are important in emulsion stabilization. Pulse proteins with low denaturation enthalpy, a feature of the pulse albumins, tend to generate smaller oil droplets, most likely due to their small particle size (4–5 nm) which enables dense pack of proteins at the oil-water interface and promote the formation of stiff protein network structure that helps to stabilize the newly generated oil droplets during/after homogenization. High thermal stability, as observed in pulse legumin globulins, is detrimental to the interfacial stiffness, and the resistance of the interfacial network structure to large deformations due to the lack of protein-protein in-plane interactions and tend to give low emulsion stability under high shear blending. During emulsion storage, pulse albumins tend to cause droplet flocculation/coalescence also in the whole protein mixtures, likely due to their low surface charge and smaller particle size that could not provide enough electrostatic and steric repulson. Overall, albumins dominate the emulsion stability of pulse proteins under high shear blending, and globulins dominate the emulsion storage stability. This study may help to guide the screening of pulse proteins for desired emulsifying properties. The proposed key molecular and interfacial parameters could be used for further modeling, for example, based on artificial intelligence, to better understand and predict the functionalities of pulse proteins in multiphase systems.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111463"},"PeriodicalIF":11.0,"publicationDate":"2025-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143873227","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pectin emulsion gel: Effect of different low-methoxyl pectin on loading and colon-targeted release of curcumin","authors":"Muhammad Muntaqeem Arain ,&nbsp;Ruoxuan Li ,&nbsp;Qin Chen ,&nbsp;Shuixian Huang ,&nbsp;Yanbing Zhang ,&nbsp;Yitong Liu ,&nbsp;Siyi Pan ,&nbsp;Fengxia Liu","doi":"10.1016/j.foodhyd.2025.111461","DOIUrl":"10.1016/j.foodhyd.2025.111461","url":null,"abstract":"<div><div>High hydrostatic pressure-assisted enzymatic de-esterification of pectin (HHP-pectin) significantly enhanced the emul-gelling properties of low-methoxyl pectin (LMP). However, the effect of HHP-pectin-based emulsion gel on loading and controlled delivery has not been explored yet. In this study, emulsion gels of HHP-pectin were loaded with curcumin, and alkaline de-esterified LMP (A-pectin) with DM 5∼10 % was used as a control. It was found that curcumin was well encapsulated in LMP emulsion gel structure, and the encapsulation efficiency (EE) increased significantly, reaching 92.55 ± 2.19 %. At the same DM (5∼10 %), emulsion gel of HHP-pectin had more dense structure with uniform packing than that of A-pectin, that significantly improved light and thermal stability of curcumin, with retention rate of about 70.91 ± 1.07 % and 79.91 ± 2.35 % after 18 h of ultraviolet light treatment and 90 min of thermal treatment, respectively. LMP emulsion gels could significantly inhibit the release of curcumin in the oral, stomach, and small intestine, and at lower DM, it had a better-sustained release effect in the colon. At the same DM, HHP-pectin had a higher and sustained release of curcumin (89.03 ± 0.76 %) in the colon than A-pectin, mainly attributed to higher molecular weight (Mw) and viscosity of HHP-pectin. Thus, these results suggested that HHP significantly improved the potential of LMP emulsion gels as an effective carrier for colon-targeted delivery and its application in the food and drug industries.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111461"},"PeriodicalIF":11.0,"publicationDate":"2025-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143855730","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mechanistic insights into the stabilization of caseinglycomacropeptide foams via chia mucilage incorporation","authors":"K. Saporittis,&nbsp;R. Morales,&nbsp;M.J. Martinez","doi":"10.1016/j.foodhyd.2025.111458","DOIUrl":"10.1016/j.foodhyd.2025.111458","url":null,"abstract":"<div><div>Chia seed mucilage (CM) is a new and sustainable edible plant hydrocolloid that exhibits a variety of techno-functional, nutritional and healthy properties that make it a valuable ingredient in food development. One of its potential aptitudes is its use as a stabilizer in colloidal systems, for this reason this study proposes to explore the use of CM as a foam stabilizing agent, particularly in mixtures with caseinglycomacropeptide (CMP), a dairy peptide with great foaming capacity but a poor stability. For this purpose, interaction and interfacial studies were carried out, as well as the evaluation of the foam-forming and foam-stabilizing capacity.</div><div>In this study, it was confirmed that CM can be used as a stabilizer for CMP foams and two mechanisms that regulate this stability were identified: 1) the contribution to the increase in viscosity of the continuous phase, which was greater at higher CM concentration, both at pH 7 (2.61–3.7 mPa s, for 0.1 % w/w and 10.17–23.3 mPa s, for 0.5 % w/w) and 3 (2.7 mPa s, for 0.1 % w/w and 7.57–19.3 mPa s, for 0.5 % w/w), increasing the viscosity of the liquid in the lamella border and slowing down the liquid drainage and the bubbles coalescence; 2) the improvement of the rheological properties of the interfacial film (with elastic modulus values about 45–55 mN/m for CMP-CM versus 20–35 mN/m for individual components) by the synergistic performance of the CMP-CM complex at the air-water interface, which occurs under conditions where the biopolymers have opposite charges (pH 3), promoting the formation of a more elastic and resistant film, which avoid the foam collapse. These findings can be exploited to a better design of a stable foam in real products, with the advantage that using a novel ingredient with numerous reported health benefits.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111458"},"PeriodicalIF":11.0,"publicationDate":"2025-04-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143873236","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mechanistic insights into arginine-mediated gluten solubility enhancement and aggregation inhibition across specific subunit and molecular scales","authors":"Tao Yang ,&nbsp;Tian Lv ,&nbsp;Bo Wang ,&nbsp;Yue Zhang ,&nbsp;Pei Wang ,&nbsp;Qin Zhou ,&nbsp;Dong Jiang ,&nbsp;Ping-ping Zhang ,&nbsp;Hao Jiang","doi":"10.1016/j.foodhyd.2025.111451","DOIUrl":"10.1016/j.foodhyd.2025.111451","url":null,"abstract":"<div><div>This study elucidates the mechanisms by which arginine (Arg⁺) inhibits gluten aggregation and enhances solubility, focusing on individual high-molecular-weight glutenin subunit (HMW-GS) using a set of HMW-GS deletion lines. Comparative analyses with Arg⁺, guanidine (Gdn⁺), and glycine (Gly) demonstrated increased solubility in HMW-GS deletion lines compared to wild type, particularly under Arg⁺ and Gdn⁺, following the order for HMW-GS deletion at: <em>Bx7 &gt; By8 &gt; Ax1 &gt; Dy12 &gt; Dx2</em>. Arg ⁺ enhanced solubility by quenching gluten structure, primarily restructuring hydrogen bonds, weakening hydrophobic interactions, destabilizing β-sheets, and facilitating β-turn and β-sheet transitions, alongside shifts from ggg to the least stable disulfide bond conformation (tgt). Molecular dynamics simulations revealed the heightened sensitivity of <em>Dx2</em> to Arg⁺, driven by guanidino-mediated interactions and local crowding effects. These findings highlight the dominant role of the guanidino group in solubility enhancement, with carboxyl and alkyl groups playing supporting roles.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111451"},"PeriodicalIF":11.0,"publicationDate":"2025-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143855111","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effects of milk protein concentrate decalcification on casein micelles as carriers for lutein","authors":"Bing Hu ,&nbsp;Xin Chen ,&nbsp;Ruiyi Zhai ,&nbsp;Peter A. Williams ,&nbsp;Jianming Guo ,&nbsp;Jixin Yang ,&nbsp;Wei Wang ,&nbsp;Nuo Dong ,&nbsp;Lingyu Han ,&nbsp;Jijuan Cao","doi":"10.1016/j.foodhyd.2025.111457","DOIUrl":"10.1016/j.foodhyd.2025.111457","url":null,"abstract":"<div><div>The effects of partial calcium depletion of milk protein concentrates (MPC) on the dissociation of casein micelles were investigated. MPC after decalcification with varying calcium content (0.93, 0.80, 0.69, 0.53, 0.41 and 0.39 mmol/L) were produced by ion-exchange treatment. The compositions and structural properties of the concentrates were analyzed using SDS-PAGE, UV–Vis absorption and fluorescence spectroscopy, circular dichroism spectroscopy, X-ray diffraction, and measurement of surface hydrophobicity. Although the decalcification treatment had no effect on the protein composition of MPC, it was found to influence the micellar micromorphology of the casein micelles, as shown by transmission electron microscopy. Decreases in calcium content from 0.93 to 0.41 mmol/L were associated with reductions in the sizes of the micelles which were spherical in shape. The micelles delete changed shape at 0.39 mmol/L (calcium content). The zeta potential of MPC and decalcified MPC micelles changed as calcium concentration decreased. Decalcified MPC with the lowest calcium content had the highest surface charge, with differences in surface charge likely influencing micelle dissociation. The decalcification of MPC significantly influenced the loading and release of lutein by the micelles. At 0.69 mmol/L calcium content, MPC micelles had well-dispersed spherical shapes with markedly smaller particle size, together with the highest loading capacity and encapsulation efficiency. Simulated digestion showed that the micelles of moderately decalcified milk protein concentrates promoted lutein stability and its release in the intestine. These findings open up the possibility of fabricating MPC with customized functionality, especially in the delivery of fat-soluble pigments in food industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111457"},"PeriodicalIF":11.0,"publicationDate":"2025-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143843349","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Alginate-pectin microparticles embedding self-assembling antimicrobial peptides and resveratrol for antimicrobial and anti-inflammatory applications","authors":"Cesar Augusto Roque-Borda ,&nbsp;Marco Roberto Chávez-Morán ,&nbsp;Laura Maria Duran Gleriani Primo ,&nbsp;José C.E. Márquez Montesinos ,&nbsp;Vinicius Martinho Borges Cardoso ,&nbsp;Mauro M.S. Saraiva ,&nbsp;Caroline Maria Marcos ,&nbsp;Marlus Chorilli ,&nbsp;Fernando Albericio ,&nbsp;Beatriz G. de la Torre ,&nbsp;Fernando Rogério Pavan ,&nbsp;Andréia Bagliotti Meneguin","doi":"10.1016/j.foodhyd.2025.111454","DOIUrl":"10.1016/j.foodhyd.2025.111454","url":null,"abstract":"<div><div>Integrating antimicrobial peptides (AMPs) into alginate-pectin-based microstructured delivery systems enhances the controlled release and stability of bioactive like resveratrol. This study examines spray-dried microparticles utilizing alginate and pectin as primary carbohydrate polymers combined with aggregated AMPs for dual antioxidant and antimicrobial effects. The AMP was self-assembled into nanostructures upon interaction with alginate and pectin, which were subsequently incorporated into spray-dried microparticles, resulting in a stable delivery system. <em>In silico</em> modeling and <em>in vitro</em> release studies under simulated gastrointestinal conditions showed that AMP-containing microparticles provided a slower, sustained resveratrol release than peptide-free systems. The Weibull model best described the release, indicating a multi-phase behavior driven by diffusion and erosion. In gastric simulated conditions, the alginate-pectin matrices with AMP improved structural integrity, reducing release, while in intestinal ones, partial erosion enabled controlled release. <em>In vivo</em> infection studies using <em>Galleria mellonella</em> demonstrated significant reductions in inflammation and bacterial load 48 h post-infection. These results suggest that alginate-pectin microparticles with aggregated AMPs enhance the antioxidant release and maintain antimicrobial activity, making them promising for gastrointestinal applications. According to these promising findings, the next step studies will aim to enhance site-specific therapeutic performance through formulation refinement and targeted delivery strategies.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111454"},"PeriodicalIF":11.0,"publicationDate":"2025-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143867902","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structure-function relationship and antioxidant mechanisms of pectin from red and white pitaya peels for functional food applications","authors":"Tainara Araujo Amorim ,&nbsp;Ana Julia de Brito Araujo Carvalho ,&nbsp;Luana da Silva Figueiredo ,&nbsp;Marcos dos Santos Lima ,&nbsp;Ana M. Sarinho ,&nbsp;Newton Carlos Santos ,&nbsp;Hugo M. Lisboa ,&nbsp;Thaisa Abrantes Souza Gusmão ,&nbsp;Rennan de Pereira Gusmão","doi":"10.1016/j.foodhyd.2025.111455","DOIUrl":"10.1016/j.foodhyd.2025.111455","url":null,"abstract":"<div><div>Natural valorization of agricultural by-products is increasingly important for developing sustainable functional foods. This study aimed to investigate the antioxidant potential and quantitative structure-activity relationship (QSAR) of pectin extracted from red (<em>Hylocereus polyrhizus</em>) and white (<em>Hylocereus undatus</em>) pitaya peels, with a focus on elucidating their functional applications in food and nutraceutical formulations. Red pitaya pectin (RP) had a higher degree of methyl-esterification (73.5 %) than white pitaya pectin (WP, 61.3 %), contributing to distinct antioxidant profiles. RP showed stronger ferric reducing antioxidant power (FRAP, 4.10 mmol Fe²⁺/kg), whereas WP exhibited superior DPPH radical scavenging activity (1.47 mmol Trolox/kg). Key phenolic compounds—isorhamnetin (3.14 mg/kg) and procyanidin A2 (1.09 mg/kg) in RP, and myricetin (1.38 mg/kg) and kaempferol 3-glucoside (1.20 mg/kg) in WP—were identified as major contributors to antioxidant efficacy. QSAR modeling emphasized how matrix properties, particularly degree of methyl-esterification and molecular weight, regulate phenolic accessibility. Specifically, the denser RP matrix restricted phenolic mobility and favored lipophilic compounds, while WP's more porous structure enhanced hydrophilic phenolic interactions. Both matrices exhibited low synergy indices, underscoring complex matrix effects on antioxidant activity. Overall, the findings highlight pitaya peel pectin as promising natural antioxidants suitable for diverse functional food applications. By converting underutilized fruit waste into high-value hydrocolloids, this work supports sustainable practices and the circular economy, paving the way for innovative, eco-friendly formulations in the food industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111455"},"PeriodicalIF":11.0,"publicationDate":"2025-04-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143851969","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antioxidant, UV-blocking, and biodegradable pectin films containing selenium nanoparticles for sustainable food packaging","authors":"Guilherme A.M. Jesus ,&nbsp;Michael C. Castro ,&nbsp;Paulo R. Souza ,&nbsp;Johny P. Monteiro ,&nbsp;Roberta M. Sabino ,&nbsp;Shyam S. Sablani ,&nbsp;Alessandro F. Martins ,&nbsp;Elton G. Bonafé","doi":"10.1016/j.foodhyd.2025.111449","DOIUrl":"10.1016/j.foodhyd.2025.111449","url":null,"abstract":"<div><div>Traditional plastic packaging is a significant contributor to environmental pollution, emphasizing the urgent need for sustainable alternatives. This study focuses on the development and characterization of biodegradable pectin-based films functionalized with selenium nanoparticles (SeNPs). The films were prepared using the casting method and subjected to extensive characterization. Biodegradability tests indicated that the films lost their integrity within six days. Optical analyses (color, opacity, and UV barrier) showed that transparent films with a slight orange hue (due to SeNPs) and UV-blocking properties were successfully produced. Structural and morphological alterations induced by the incorporation of Ca²⁺ and SeNPs were confirmed through X-ray diffraction, atomic force microscopy (AFM), and scanning electron microscopy. AFM provided insights into roughness, adhesion energy, adhesion force, deformation, equivalent Young's modulus, and electrostatic force. Mechanical and swelling tests further corroborated these findings. Calcium-crosslinked films containing SeNPs exhibited enhanced tensile strength (9.11−12.68 MPa), flexibility (10.58−25.18 %), and swelling capacity (1336−1649 %), especially at SeNP concentration of 0.4 % and 0.8 %. The performance of these films was evaluated by assessing the shelf life of fresh strawberries. Uncoated fruits showed signs of microbial growth by the third day, while film-coated fruits exhibited clean surfaces and reduced mass change. This preservation effect is attributed to the antioxidant activity of selenium, primarily when SeNPs with a reduced particle size (≈50 nm, as characterized by transmission electron microscopy) were used. Moreover, cytotoxicity tests confirmed that the films are safe for use in food packaging. In conclusion, calcium-crosslinked pectin-based films functionalized with SeNPs offer great potential for improving food preservation while contributing to environmental sustainability through biodegradable packaging solutions.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111449"},"PeriodicalIF":11.0,"publicationDate":"2025-04-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143838449","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to “Hybrid Carrageenans from Betaphycus gelatinus: Physicochemical and rheological properties” [Food Hydrocolloids 166 (2025) 111296]","authors":"Sanjida Humayun ,&nbsp;Amal D. Premarathna ,&nbsp;Vitalijs Rjabovs ,&nbsp;Marius Benoit ,&nbsp;Indrek Reile ,&nbsp;Alan T. Critchley ,&nbsp;Michael Y. Roleda ,&nbsp;Rando Tuvikene","doi":"10.1016/j.foodhyd.2025.111418","DOIUrl":"10.1016/j.foodhyd.2025.111418","url":null,"abstract":"","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111418"},"PeriodicalIF":11.0,"publicationDate":"2025-04-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143823874","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of combined pH-Shifting and high-intensity ultrasound treatment on the structural, functional, and foaming properties of Tenebrio Molitor Protein","authors":"Dongjie Huang ,&nbsp;Wenyuan Zhang ,&nbsp;Yiyan Liu ,&nbsp;Jingkai Zhang ,&nbsp;Yang Jiang ,&nbsp;Qingrong Huang ,&nbsp;Dapeng Li","doi":"10.1016/j.foodhyd.2025.111384","DOIUrl":"10.1016/j.foodhyd.2025.111384","url":null,"abstract":"<div><div>With the development of the food industry and the increasing variety of emerging foods, the foaming properties of proteins have gained attention in the production of blowing agents. As a novel source of protein supplementation, insect protein has recently garnered widespread interest for its applications in food. However, Tenebrio Molitor Protein (TMP) has not been utilized in the production of aerated foods due to its inherently poor water-air interfacial properties. To improve the foaming properties of TMP, a combined modification treatment involving extreme pH-shifting and high-intensity ultrasound (HIUS) was applied. The results showed that under highly alkaline conditions, TMP is more susceptible to the effects of HIUS. Under these conditions, protein molecules unfold, and the cavitation effect of ultrasound disrupts numerous non-covalent bonds, leading to the dissociation of a significant number of soluble aggregates. This reduces the particle size of the protein, exposes hydrophobic groups, enhances surface hydrophobicity, and increases the free sulfhydryl content. Additionally, the secondary and tertiary structures of TMP were altered by the modification treatment: the content of α-helices increased, while the contents of β-turns and β-sheets decreased. These structural changes enhanced proteins' interfacial properties at the water-air interface, enabling the modified protein (UTMP-12) to achieve excellent foaming properties. This study provides a new approach for the application of TMP in aerated food products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111384"},"PeriodicalIF":11.0,"publicationDate":"2025-04-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143851968","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}