Future Foods最新文献

{"title":"Valorization of hops by-product for development of active poly(butylene succinate) film","authors":"Angela Borriello ,&nbsp;Angela Marotta ,&nbsp;Leandra Leto ,&nbsp;Martina Cirlini ,&nbsp;Benedetta Chiancone ,&nbsp;Prospero Di Pierro ,&nbsp;Veronica Ambrogi ,&nbsp;Elena Torrieri","doi":"10.1016/j.fufo.2026.100899","DOIUrl":"10.1016/j.fufo.2026.100899","url":null,"abstract":"<div><div>Hop by-product powder (HBP), obtained from milling branches, leaves, and discarded cones, was valorized as a functional additive in polybutylene succinate (PBS) films to develop biodegradable antioxidant packaging. The HBP was first characterized for water absorption/desorption capacity and particle size distribution, then separated into three fractions based on fiber size (HBP-S: 63–160 μm; HBP-M: 160–220 μm; HBP-L: 220–710 μm). Total HBP (HBP-T) and each fraction were analysed for chemical composition and antioxidant properties. Four PBS composite films containing 10 wt.% of HBP-T, -S, -M, and -L were produced via melt blending, pelletizing, and compression molding. Their optical, thermal, mechanical, barrier, and water sorption properties were evaluated, together with antioxidant activity assessed by ethanolic extraction and in contact with food simulants. Smaller HBP particles exhibited higher cellulose content (≈79%), greater polyphenol concentration (≈10 mg GAE/g_dw), and stronger antioxidant activity (≈14 mg TEAC/g_dw). Incorporating HBP enhanced the films' elastic modulus and water absorption, shifting color toward red-yellow hues, particularly with smaller fibers. Fiber size had minimal impact on mechanical and thermal properties or antioxidant retention, suggesting that fractionation may be unnecessary. HBP maintained its antioxidant properties in PBS and demonstrated different release profiles in food simulants. The antioxidant activity of films increased over time, reaching values of 1.7 mg TEAC/g_film (DPPH, 7 days) and 23 mg TEAC/g_film (ABTS, 10 days). Simulants C and D1 had a higher capacity to solubilize antioxidant compounds from the film. These findings confirm HBP’s potential to enhance PBS films functionality, making them promising for biodegradable antioxidant food packaging.</div></div>","PeriodicalId":34474,"journal":{"name":"Future Foods","volume":"13 ","pages":"Article 100899"},"PeriodicalIF":8.2,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145926005","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Optimizing culture conditions for myogenic differentiation of bovine mesenchymal stromal cells","authors":"Emma Heyman ,&nbsp;Bert Devriendt ,&nbsp;Flore De Bondt ,&nbsp;Mario Van Poucke ,&nbsp;Luc Peelman ,&nbsp;Stefaan De Smet ,&nbsp;Catharina De Schauwer","doi":"10.1016/j.fufo.2025.100893","DOIUrl":"10.1016/j.fufo.2025.100893","url":null,"abstract":"<div><div>Mesenchymal stromal cells (MSCs) are a promising alternative cell source for cultured meat production, but no robust protocols exist for farm animal MSCs to efficiently induce myogenic differentiation. Differentiation efficiency was evaluated under different conditions: normoxia versus hypoxia, with or without 5-Aza-2′-deoxycytidine (5-Aza) for 24 h versus 21 days, horse serum versus fetal bovine serum (FBS), and supplementation with galectin-1 (Gal-1) versus the combination dexamethasone + hydrocortisone. A protocol was established by supplementing 10 µM 5-Aza, 100 nM Gal-1, and 10% FBS in normoxia, as confirmed by increased mRNA levels of <em>MYF5, MYOD1, MRF4</em> and <em>MYOG</em>, decreased <em>PAX3</em>, increased desmin, tropomyosin, and MyHC protein levels, and formation of myotube-like structures, as indicated by the presence of multinucleated cells. To study breed effects, bovine MSCs from Holstein Friesian (HF) and Belgian Blue (BB) were myogenically differentiated. Differences were observed with <em>MYOG</em> expression and MyHC expression being higher in BB-MSCs, although fusion into multinucleated myotubes was limited. Additionally, immunophenotypic profiles of HF-MSCs and BB-MSCs were assessed before and after myogenic differentiation. Following myogenic differentiation, significant reduction of MSC markers (CD29, CD44, CD90, and CD34) was observed. Our findings lay the foundation for further studies aimed at optimizing myogenic differentiation of MSCs.</div></div>","PeriodicalId":34474,"journal":{"name":"Future Foods","volume":"13 ","pages":"Article 100893"},"PeriodicalIF":8.2,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145926007","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antioxidant peptide from Synechococcus marine microalgae with therapeutic potential against human colon adenocarcinoma","authors":"Tanatorn Saisavoey ,&nbsp;Patamalai Boonserm ,&nbsp;Papassara Sangtanoo ,&nbsp;Piroonporn Srimongkol ,&nbsp;Aphichart Karnchanatat","doi":"10.1016/j.fufo.2025.100895","DOIUrl":"10.1016/j.fufo.2025.100895","url":null,"abstract":"<div><div>The research focuses on the peptide AILQSYSAGKTK (AK-12), synthesized from the marine microalga <em>Synechococcus</em>, to determine its antioxidant and apoptotic properties. Antioxidant activity is attributed to residues like tyrosine and glutamic acid, which chelate metal ions and neutralize free radicals. <em>In silico</em> analysis indicates that AK-12 is non-toxic, non-allergenic, and suitable for oral consumption, despite poor intestinal permeability. According to circular dichroism (CD) analysis, AK-12 predominantly adopts a random coil structure. AK-12 reduced Caco-2 cell viability in a dose-dependent manner and lowered intracellular ROS, confirming notable antioxidant activity. Molecular docking analysis indicated that AK-12 exhibits a strong binding affinity for Bcl-2, suggesting its potential to inhibit the protein’s anti-apoptotic functions. Flow cytometry confirmed that AK-12 induced apoptosis in Caco-2 cells dose-dependently. Flow cytometry indicated dose-dependent apoptosis, supported by RT-qPCR results showing upregulation of caspase-8 and caspase-9 mRNA, and a moderate increase in caspase-3. Western blot analysis further substantiated these findings by showing increased expression of Bax, and caspase-9, coupled with reduced Bcl-2 levels, confirming the mitochondrial pathway’s central role in apoptosis induction. These findings suggest that AK-12 has potential as a functional food ingredient for colon cancer treatment due to its dual antioxidant and pro-apoptotic activities.</div></div>","PeriodicalId":34474,"journal":{"name":"Future Foods","volume":"13 ","pages":"Article 100895"},"PeriodicalIF":8.2,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145926594","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization and in vitro digestive properties of potato starch gels enhanced with soy protein fiber aggregates","authors":"Meiqi Xu ,&nbsp;Siqian Chen ,&nbsp;Yuge Zhang ,&nbsp;Antuan Sun ,&nbsp;Huannan Li ,&nbsp;Xiaolu Guo ,&nbsp;Zhuoqi Wu ,&nbsp;Mengyang Chen ,&nbsp;Xu Chen ,&nbsp;Jie Zhu","doi":"10.1016/j.fufo.2025.100886","DOIUrl":"10.1016/j.fufo.2025.100886","url":null,"abstract":"<div><div>In recent years, dysphagia has become increasingly prevalent as a geriatric syndrome, often leading to complications such as malnutrition and esophageal injury. To address this issue, this study developed a novel starch–protein composite gel with low digestibility and high swallowing safety using soy protein fibril aggregates (SPFA) and potato starch (PS). The <em>in vitro</em> digestibility, microstructure, textural, and rheological properties of the composite gel were systematically evaluated. Results showed that increasing SPFA content improved the gel's elasticity, cohesiveness, and chewiness, though it slightly reduced its water-holding capacity. The SPFA enhanced hydrophobic and hydrogen-bonding interactions within the gel matrix, reinforcing its solid-like behavior through a composite network stabilized primarily by electrostatic, hydrophobic, and hydrogen bonding. Notably, the incorporation of 0.2% SPFA significantly reduced rapidly digestible starch content to 76.43% and increased resistant starch to 22.95%, attributed to the reinforced network limiting enzymatic accessibility. These findings demonstrate that the SPFA–PS composite gel possesses desirable anti-digestive properties and a soft texture, showing strong potential as a nutritious and health-oriented food material for populations with dysphagia.</div></div>","PeriodicalId":34474,"journal":{"name":"Future Foods","volume":"13 ","pages":"Article 100886"},"PeriodicalIF":8.2,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145926596","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Enhancement of chitosan/gelatin biodegradable films with cashew nut skin extract and Ocimum gratissimum L. essential oil for active food packaging","authors":"Xuan-Tien Le ,&nbsp;Quy Sinh Nguyen ,&nbsp;Minh-Tam K. Nguyen ,&nbsp;Thi Quynh Ngoc Nguyen","doi":"10.1016/j.fufo.2025.100867","DOIUrl":"10.1016/j.fufo.2025.100867","url":null,"abstract":"<div><div>Excessive use of petroleum-based plastics in food packaging has sparked environmental and health concerns, prompting demand for sustainable alternatives like biodegradable active films that reduce ecological impact, enhance safety, and extend shelf life. In this study, cashew nut skin extract (CNSE) and <em>Ocimum gratissimum</em> L. essential oil (OGEO) were incorporated into chitosan/gelatin-based films, either individually or in combination, to develop active biodegradable packaging films with enhanced functionalities. Compared to the control film (CG00), the CG03 film with 3 % CNSE addition showed improved water resistance, antimicrobial properties, and thermal stability, while maintaining a compact microstructure, although it had reduced flexibility. Conversely, the CG10 film with 1 % OGEO addition exhibited enhanced antioxidant activity and mechanical performance, but with a more porous microstructure, lower thermal stability, and increased water vapor permeability. Notably, the CG13 film containing both OGEO and CNSE exhibited significantly better overall performance than films formulated with either component alone. The CG13 film demonstrated 1.1 and 35.3 times higher antioxidant activity in the ABTS assay compared to CG10 and CG03, respectively, while also exhibiting superior antimicrobial activity, optical properties, and a balanced profile of mechanical strength, moisture resistance, and thermal stability. Remarkably, CG13 outperformed CG00, CG10 and CG03 in preserving the quality of fresh pork. After 13-days storage, the TVB-N value of fresh pork wrapped with CG13 was 19 %, 8 % and 11 % lower than that wrapped with CG00, CG10 and CG03, respectively. These findings highlight the potential of combining OGEO and CNSE to develop sustainable, high-performance active food packaging materials.</div></div>","PeriodicalId":34474,"journal":{"name":"Future Foods","volume":"13 ","pages":"Article 100867"},"PeriodicalIF":8.2,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145791509","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Selective production of novel ACE-inhibitory peptides from brewer’s spent grain via two-stage enzymatic hydrolysis and integrated fractionation","authors":"Parichat Paksin ,&nbsp;Korrawan Sringarm ,&nbsp;Pipat Tangjaidee ,&nbsp;Wannaporn Klangpetch ,&nbsp;Pornchai Rachtanapun ,&nbsp;Ekasit Onsaard ,&nbsp;Jaksuma Pongsetkul ,&nbsp;Saroat Rawdkuen ,&nbsp;Young Hoon Jung ,&nbsp;Jinhu Tian ,&nbsp;Suphat Phongthai","doi":"10.1016/j.fufo.2025.100877","DOIUrl":"10.1016/j.fufo.2025.100877","url":null,"abstract":"<div><div>Brewer's spent grain represents an underutilized protein source capable of yielding bioactive peptides with potential health benefits, supporting food system sustainability, aligning with an environmental management system, and contributing to environment and health. This study aimed to optimize the release of Angiotensin-I Converting Enzyme (ACE)-inhibitory peptides from brewer's spent grain proteins through enzymatic hydrolysis using Flavourzyme and Alcalase, both individually and in a sequential manner. Peptides generated via selective Alcalase-Flavourzyme hydrolysis exhibited significant bioactivities (<em>p</em> &lt; 0.05), including ABTS radical scavenging (381.91 ± 6.93 μmoL Trolox equivalent/g sample), metal chelation (1128.34 ± 19.45 μmoL EDTA/g sample), and ACE-inhibitory activity (IC₅₀, 0.11 ± 0.01 mg/mL). Peptides were further separated using membrane ultrafiltration into four fractions based on molecular weight: &lt;3 kDa, 3–5 kDa, 5–10 kDa, and &gt;10 kDa. The &lt;3 kDa fraction showed the highest ACE-inhibitory activity (IC₅₀, 74.68 ± 0.28 μg/mL, <em>p</em> &lt; 0.05). The most active fraction underwent size exclusion chromatography and Liquid Chromatography-Tandem Mass Spectrometry to determine amino acid sequences. Hydrophobic residues, including valine, proline, glycine, and leucine, were prevalent in four identified peptides (GDRLL, LPTHL, VPFVVPGSE, and VPFVPGSVE), contributing to ACE inhibition. The combined two-stage enzymatic hydrolysis and integrated fractionation within the manufacturing process significantly enhanced ACE-inhibitory activity, achieving approximately 1500-fold improvement compared to non-hydrolyzed protein. Bioactive peptides derived from brewer's spent grain protein hydrolysates may serve as sustainable, high-value ingredients, supporting healthy diets and innovative applications in food and nutraceutical products.</div></div>","PeriodicalId":34474,"journal":{"name":"Future Foods","volume":"13 ","pages":"Article 100877"},"PeriodicalIF":8.2,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145791536","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Impact of pre-treatments assisted controlled germination and infrared drying on the functional, bioactive components and antinutritional properties of Moringa oleifera seeds","authors":"Palwasha Gul,&nbsp;Jabir Khan,&nbsp;Qingyun Li,&nbsp;Kunlun Liu","doi":"10.1016/j.fufo.2025.100865","DOIUrl":"10.1016/j.fufo.2025.100865","url":null,"abstract":"<div><div>Controlled germination is an effective strategy to enhance the quality profile of <em>Moringa oleifera</em> (MO) seeds. This study investigated the influence of dual-frequency ultrasound and microwave-assisted controlled germination (Biochemical Incubator, 25 °C, 15 days), followed by infrared vacuum drying at 70, 60, and 50 °C on MO seeds quality. Functional, mineral, phenolic, flavonoid, and structural properties were comprehensively evaluated. Ultrasonication significantly improved gel formation, water absorption capacity, oil absorption capacity, and other functional properties (<em>P</em> ≤ 0.05). In term of minerals compositions, US10 &amp; 20 samples dried at 50 &amp; 60 °C increased Mg by 16.07 % and Ca by 21.67 %, while K and Na remained stable. In contrast, drying at 70 °C decreased the content of Ca, Fe and Mg by 58.11 %, 2.35 % and 12.17 %, respectively. Mineral composition in US samples was significantly higher than MW, and both were significantly higher when compared with control samples. Regarding the phenolic acid profile, US10 at 60 °C yielded the highest hydroxycinnamic acids and flavonoids, while US20 at 50 °C yielded the hydroxybenzoic content, overall exhibited 1.78–2.41-fold increase in phenolic acids profile of MO seeds. Antinutritional factors decreased significantly, with phytic acid reduced by 42.12–77.64 % and tannins by 46.20–74.51 %. Overall, samples dried at 70 °C demonstrated poor quality attributes. Structural analyses (XRD, FTIR) revealed molecular modifications, with the relative crystallinity of US20 slightly increased from 16.62 % to 36.27 % as compared to control. In contrast, the crystallinity of OGS, US10, MW30, and MW60 samples decreased, ranging from 7.68 % to 19.05 %, indicating structural changes. These alterations suggest enhanced signal transmission in the pre-treated samples compared to the control. SEM analysis confirmed aggregation of germinated MO seeds across drying conditions, showing a film-like structure where starch aggregates coupled with lipids embedded within a protein matrix.</div></div>","PeriodicalId":34474,"journal":{"name":"Future Foods","volume":"13 ","pages":"Article 100865"},"PeriodicalIF":8.2,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145705692","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Anthocyanin-rich functional drinks enriched with hyaluronic acid (HA) and hydrolysed marine collagen: Physicochemical, antioxidant, and toxicity evaluation","authors":"Deia Tawalbeh ,&nbsp;Nur Fatieha Ismail ,&nbsp;Soon Yong Ing ,&nbsp;Nur Abir Dzulkifli ,&nbsp;Mohd Hafiz Mail ,&nbsp;Nur Hasnieza Mohd Rosli ,&nbsp;Faisalina Ahmad Fisol ,&nbsp;Norizah Mhd. Sarbon","doi":"10.1016/j.fufo.2026.100917","DOIUrl":"10.1016/j.fufo.2026.100917","url":null,"abstract":"<div><div>This study examined anthocyanin-rich drinks containing hyaluronic acid (HA) and varying concentrations of hydrolyzed marine collagen (HMC) (0–5 %), formulated to assess their physicochemical properties, antioxidant and anti-tyrosinase activities, sensory acceptability, collagen content, and toxicity profile. The results indicated that increasing the concentration of HMC led to higher turbidity, total soluble solids, antioxidant, and anti-tyrosinase activity, as well as increased mineral, protein, fiber, and ash content. Notably, the addition of 2.5 % HMC received the highest overall acceptability score, second only to the control. This concentration also enhanced the total collagen content, <em>in vitro</em> collagen levels, and collagen bioavailability. A single oral administration of 2000 mg/kg of the anthocyanin-rich drink enriched with HMC over 14 days did not result in any signs of acute toxicity, indicating an LD₅₀ value greater than 2000 mg/kg.</div></div>","PeriodicalId":34474,"journal":{"name":"Future Foods","volume":"13 ","pages":"Article 100917"},"PeriodicalIF":8.2,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146078018","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mixed interfacial stabilisation of emulsions by homogenised bacterial suspensions","authors":"Yi Ling Chin ,&nbsp;Remko M. Boom ,&nbsp;Julia K. Keppler","doi":"10.1016/j.fufo.2026.100916","DOIUrl":"10.1016/j.fufo.2026.100916","url":null,"abstract":"<div><div>Microbial proteins are increasingly explored as a novel food ingredient. Previous studies have shown that gentle homogenisation methods produce stable emulsions while keeping biomasses intact. However, these emulsions have large droplet sizes which may cause instability. Applying high-energy methods can improve their stability but the microbial biomass may rupture and release intracellular material that alters the emulsion stability. To assess this effect, we investigated the impact of high-pressure disruption on Gram-positive bacterial cells and its influence on emulsion stability. Bacterial cells were disrupted under conditions comparable to high-pressure emulsification. The resulting suspension was examined for the extent of disruption based on cell size, structure, composition and surface properties. Subsequently, the disrupted cell suspension was fractionated before preparing emulsions containing 10% oil and studying selected emulsion characteristics. High-pressure treatment deagglomerated and ruptured the cells, resulting in a soluble surface-active fraction, but only about 3% of the bacterial proteins were solubilised. Surface hydrophobicity increased but charge was reduced in the biomass after treatment. Oil-in-water emulsions prepared using either the soluble or insoluble fraction of the suspension creamed during storage, whereas the emulsion containing both fractions remained stable for up to 14 days, indicating that emulsion stability is enhanced by both fractions. We assume a combination of particle (protein aggregates) and molecular effects (solubilised proteins and surface-active components) stabilising the interface under these circumstances. This study offers an integrated approach to disrupt bacterial cells and produce stable emulsions without further purification. Insights into the stabilisation mechanisms for each system are proposed.</div></div>","PeriodicalId":34474,"journal":{"name":"Future Foods","volume":"13 ","pages":"Article 100916"},"PeriodicalIF":8.2,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146078017","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pea protein-derived peptides as antagonists of T2R4, T2R7, and T2R14 human bitter taste receptors","authors":"Deepak Kadam ,&nbsp;Nisha Singh ,&nbsp;Vikram Bhatia ,&nbsp;Adeola M. Alashi ,&nbsp;Prashen Chelikani ,&nbsp;Rotimi E. Aluko","doi":"10.1016/j.fufo.2026.100919","DOIUrl":"10.1016/j.fufo.2026.100919","url":null,"abstract":"<div><div>Rising concerns over excessive sugar intake and its health risks drive the need for sustainable alternatives. Food protein-derived peptides offer a potential bioactive approach, reducing sugar dependency by modulating taste perception through bitter taste receptor (T2R) antagonism. This study determined the bitter taste-masking potential of pea protein hydrolysate (PPH), using human sensory panel, electronic tongue analysis, and cell-based assays to assess the inhibition of bitter taste receptors (T2Rs). Taste panel evaluation showed that the PPH at 10 mg/mL significantly (<em>p</em> &lt; 0.05) reduced bitterness intensity of a quinine solution from an unacceptable level to acceptable. RP-HPLC fractionation of the PPH revealed two hydrophilic fractions that significantly inhibited quinine and diphenhydramine induced calcium mobilization in HEK293T cells expressing T2R4, T2R7, and T2R14, confirming receptor-specific antagonism. LC-MS/MS analysis identified six key peptides (SSGVD, KKPPASAAP, AAPAGHG, GHPDNGNC, KKSLL, and DDPD) among which GHPDNGNC, SSGVD and KKSLL showed potent antagonistic activity against quinine and diphenhydramine activation of T2R14<strong>.</strong> Electronic tongue analysis showed that KKSLL, GHPDNGNC, and SSGVD exhibited 100% suppression of quinine bitterness while they reduced diphenhydramine bitterness by 78.8%, 73.1%, and 69.1%, respectively. These peptides also inhibited angiotensin-converting enzyme activity, with SSGVD showing the strongest effect (IC₅₀ = 138.46 ± 5.21 µM). Taken together, pea protein-derived peptides represent multifunctional agents that can modulate bitterness perception while providing additional health benefits such as potential antihypertensive effects, supporting applications in developing functional, low-sugar, and sustainable food systems.</div></div>","PeriodicalId":34474,"journal":{"name":"Future Foods","volume":"13 ","pages":"Article 100919"},"PeriodicalIF":8.2,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146078016","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}