International Dairy Journal最新文献

{"title":"Biocontrol of Listeria monocytogenes in milk: Isolation and characterization of a novel bacteriophage cocktail","authors":"Gizem Cufaoglu ,&nbsp;Ayse Nur Erdinc ,&nbsp;Ilgın Ata Vural ,&nbsp;Gorkem Cengiz ,&nbsp;Bahar Onaran Acar ,&nbsp;Gultekin Unal ,&nbsp;Muammer Goncuoglu ,&nbsp;Irfan Erol ,&nbsp;Naim Deniz Ayaz","doi":"10.1016/j.idairyj.2026.106583","DOIUrl":"10.1016/j.idairyj.2026.106583","url":null,"abstract":"<div><div><em>Listeria monocytogenes</em> is a significant foodborne pathogen known for its persistence in food processing environments and resistance to various stress conditions. This study aimed to isolate and characterize bacteriophages specific to <em>L. monocytogenes</em> and evaluate their potential as biocontrol agents in milk. A total of 43 phages were isolated from diverse wastewater sources across Türkiye. Based on their host range, lytic activity, and growth kinetics, two phages (LM1116TR and LM1418TR) were selected for further comprehensive phenotypic and genomic characterization. Host range assays revealed high specificity toward <em>L. monocytogenes</em>, with lytic activity observed against multiple serotypes (1/2a, 1/2b, 1/2c, and 4b). Transmission electron microscopy revealed that the phages exhibit a myovirus-like morphotype and belong to the class <em>Caudoviricetes</em>. Whole-genome sequencing confirmed that two phages had complete circular genomes lacking antimicrobial resistance genes. Thermal stability tests showed the phages remained detectable after 1 h at 40 °C, 50 °C, and 60 °C but were sensitive to acidic pH, especially to pH 3. Significant reductions in <em>L. monocytogenes</em> counts were observed following phage cocktail treatment, reaching up to 4.22 log CFU/mL in vitro (37 °C) and 1.66 log CFU/mL in UHT milk (4 °C) (p &lt; 0.001). Additionally, one-year storage tests at +4 °C, −20 °C, and −80 °C in tryptic soy broth (TSB), SM buffer, physiological saline and Tris-Buffered Saline (TBS, 1 × ) identified TSB with 20% glycerol as the most suitable for preserving phage stability at subzero temperatures. These results show the potential of new phages as effective and stable biocontrol agents against <em>L. monocytogenes</em> in food safety applications, supporting their potential as biocontrol agents, particularly within the dairy industry.</div></div>","PeriodicalId":13854,"journal":{"name":"International Dairy Journal","volume":"177 ","pages":"Article 106583"},"PeriodicalIF":3.4,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147386508","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Development and comparative study of rapid detection methods for Salmonella based on multiple molecular and immunological techniques","authors":"Jifu Ma ,&nbsp;Wei Zhang ,&nbsp;Xingmei Deng ,&nbsp;Qian Zhang ,&nbsp;Feifan Liu ,&nbsp;Changan Chen ,&nbsp;Yue Yang ,&nbsp;Xia Zhou ,&nbsp;Zhihua Sun ,&nbsp;Jia Guo ,&nbsp;Tianyi Zhao ,&nbsp;Zhen Wang ,&nbsp;Hui Zhang","doi":"10.1016/j.idairyj.2026.106582","DOIUrl":"10.1016/j.idairyj.2026.106582","url":null,"abstract":"<div><div>The detection of <em>Salmonella</em> in milk is critical for dairy safety, requiring rapid and sensitive methods. This study developed and compared three independent techniques: real-time PCR (qPCR), loop-mediated isothermal amplification (LAMP), and a gold immunochromatographic test strip (GICT), all targeting the <em>invA</em> gene. In artificially contaminated milk, qPCR achieved a detection limit of 10³ CFU/mL with no cross-reactivity against non-target bacteria. LAMP amplification was completed within 30 min at 63 °C, with detection limits of 4.17 × 10³ CFU/mL (visual) and 4.17 × 10² CFU/mL (gel electrophoresis). The GICT strip, based on monoclonal antibody 8E7 1C8, showed a detection limit of 10⁴ CFU/mL and remained stable for 6 months at 4 °C. While qPCR and LAMP offered high sensitivity suitable for laboratory quantification, GICT provided a rapid, equipment-free option for on-site screening. Together, these methods provide a complementary toolkit for detecting <em>Salmonella</em> across laboratory and field settings.</div></div>","PeriodicalId":13854,"journal":{"name":"International Dairy Journal","volume":"177 ","pages":"Article 106582"},"PeriodicalIF":3.4,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147386504","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mozzarella cheese as a vehicle for dietary fiber: Technological challenges and consumer acceptance","authors":"Claudia Antonino,&nbsp;Giuseppe Natrella,&nbsp;Davide De Angelis,&nbsp;Pietro Caliandro,&nbsp;Michele Faccia","doi":"10.1016/j.idairyj.2026.106605","DOIUrl":"10.1016/j.idairyj.2026.106605","url":null,"abstract":"<div><div>The dairy sector is constantly innovating in response to market trends and consumers' nutritional needs. This study investigated the feasibility of fortifying Mozzarella cheese with dietary fibers, specifically long-chain inulin and bamboo fiber, to enhance its nutritional profile. The research was conducted in two stages: a pilot-scale trial to assess the technological, physico-chemical, and sensory effects of fiber incorporation, followed by an industrial-scale production and consumer acceptance test of the most promising formulation. At the pilot scale, three cheese variants were produced: a control Mozzarella cheese (C), Mozzarella with 3% inulin (CI), and Mozzarella with 3% bamboo fiber (CB). The results showed that bamboo fiber significantly altered the cheese-making process, almost doubling the stretching time (6.55 min vs. 3.30 min for C) and substantially increasing moisture retention (greater than 4.75%), which consequently impacted the product's texture and imparted a distinct vegetable sensory note. In contrast, the inulin-fortified Mozzarella (CI) exhibited physico-chemical and sensory characteristics highly comparable to the traditional Mozzarella, showing minimal variations in color, texture, and flavor profile. Particularly, the hardness (N) of samples after production was 9.66, 10.38 and 12.33 for C, CI and CB, respectively, highlighting greater discrimination for the CB sample. Based on these results, the inulin-fortified cheese was selected for industrial scale-up. The industrially produced Mozzarella with inulin (MI) successfully incorporated a 3% fiber content, qualifying for the “Source of fiber” nutritional claim (Regulation (EC) No 1924/2006). A consumer test with 102 participants revealed that although the control Mozzarella cheese (MC) achieved higher ratings for overall acceptability and taste, the inulin-enriched version was perceived as texturally harder. Analysis of the preference map revealed that a significant proportion of consumers (60-80%) rated the MI product positively and found it acceptable. This study demonstrates that fortifying Mozzarella with inulin is technologically feasible and can produce a product with an enhanced nutritional profile, though consumer acceptance is influenced by sensory deviations from the traditional counterpart.</div></div>","PeriodicalId":13854,"journal":{"name":"International Dairy Journal","volume":"177 ","pages":"Article 106605"},"PeriodicalIF":3.4,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147386507","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Influence of added calcium on the rehydration behavior and processability of high-protein casein-based solutions reconstituted from micellar casein powder (MCP) and demineralized MCP","authors":"Brayan Castulovich ,&nbsp;Manon Hiolle ,&nbsp;Amandine Descamps ,&nbsp;Céline Lesur ,&nbsp;Benoit Cudennec ,&nbsp;Guillaume Delaplace","doi":"10.1016/j.idairyj.2026.106600","DOIUrl":"10.1016/j.idairyj.2026.106600","url":null,"abstract":"<div><div>This study investigated how added calcium influences the rehydration behavior and processability of high-protein casein-based solutions prepared from native micellar casein powder (MCP) and partially demineralized micellar casein powder (d-MCP). Dispersions (10% w/w protein) were standardized to three total calcium levels (72, 74, and 77 mM) at pH 6.9 and analyzed before and after a pasteurization-mimicking treatment (72 °C, 15 s). Soluble calcium, particle size distribution, viscosity, sedimentation, and heat coagulation time were measured. Results showed that MCP strongly re-adsorbed added calcium within the colloidal calcium phosphate network, maintaining a lower content of soluble calcium, whereas d-MCP displayed higher serum calcium. Consequently, d-MCP coagulated more rapidly at equivalent calcium levels, while MCP exhibited increasing viscosity and particle growth with rising calcium. At high mineral loads, both matrices converged to short coagulation times. These findings demonstrate that mineral partitioning and micellar history govern the stability of casein dispersions and highlight critical parameters for designing high-protein dairy beverages with controlled processability.</div></div>","PeriodicalId":13854,"journal":{"name":"International Dairy Journal","volume":"177 ","pages":"Article 106600"},"PeriodicalIF":3.4,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147386510","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular and functional characterization of Enterococcus faecalis OB15: A hypoallergenic and antimicrobial starter from Tunisian Rigouta cheese","authors":"Neyssene Aissaoui ,&nbsp;Takoua Ben Hlel ,&nbsp;Olfa Baccouri ,&nbsp;Leila Ben Farhat ,&nbsp;Kamel Eddine El Mecherfi ,&nbsp;Ferid Abidi","doi":"10.1016/j.idairyj.2026.106585","DOIUrl":"10.1016/j.idairyj.2026.106585","url":null,"abstract":"<div><div>Screening lactic acid bacteria from traditional foods is vital for identifying functional strains. <em>Enterococcus faecalis</em> OB15, isolated from Tunisian Rigouta cheese, was characterized for its technological, antimicrobial, and hypoallergenic properties. The strain displayed significant proteolytic activity against bovine α- and β-caseins and β-lactoglobulin, with optimal activity at pH 6.5 and 37–42 °C. Inhibitor assays indicated a metalloprotease mechanism, consistent with gelatinase (GelE) activity. <em>In silico</em> docking analyses confirmed that GelE targets immunodominant β-casein epitopes, generating fragments too short for antibody recognition. This structural degradation correlated with a 61% reduction in IgG immunoreactivity. Antimicrobial activity, assessed by agar diffusion assays, revealed inhibitory effects against both Gram-positive and Gram-negative foodborne pathogens, including <em>Escherichia coli</em> (9.5 ± 0.3 mm), <em>Listeria innocua</em> (8.5 ± 0.2 mm), <em>Staphylococcus aureus</em> (8.2 ± 0.2 mm) and <em>Salmonella</em> Typhimurium (8.0 ± 0.5 mm). In addition, the strain lacked vancomycin resistance (vanA/vanB) and histamine decarboxylase (hdc) genes. These findings highlight the potential of <em>E. faecalis</em> OB15 as a promising starter culture for the development of hypoallergenic fermented dairy products.</div></div>","PeriodicalId":13854,"journal":{"name":"International Dairy Journal","volume":"177 ","pages":"Article 106585"},"PeriodicalIF":3.4,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147386506","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comprehensive identification and absolute quantification of milk oligosaccharides in 25 commercial young child formulas","authors":"Hongyang Han ,&nbsp;Xinyi Xu ,&nbsp;Thom Huppertz ,&nbsp;Lina Zhang ,&nbsp;Peng Zhou","doi":"10.1016/j.idairyj.2026.106586","DOIUrl":"10.1016/j.idairyj.2026.106586","url":null,"abstract":"<div><div>This study comprehensively identified and quantified oligosaccharides (OSs) in 25 commercial young child formulas (YCFs) from China market. Using MALDI-TOF/TOF and UPLC-MS/MS, 196 OS structures were identified, of which 182 were common to all YCFs. The profile comprised 23 confirmed native bovine milk oligosaccharides (BMOs) while the majority (155 structures) likely originated from supplemented ingredients such as galacto-oligosaccharides (GOS) and fructo-oligosaccharides (FOS). Absolute quantification of eight OSs (2′-FL, 3-FL, LNnT, 3′-SL, 6′-SL, 3′-GL, 4′-GL, 6′-GL) revealed total abundances ranging from 1245.4 to 6728.1 μg g⁻¹. The GL isomers (3’/4’/6′-GL) were most abundant, consistent with GOS fortification, followed by the sialylated OSs (3′-SL and 6′-SL). In contrast, 2′-FL, 3-FL, and LNnT were present at relatively low levels. Clarifying OS origins along with their abundance is fundamental to a comprehensive understanding of YCFs, enabling accurate functional assessment and targeted product enhancement.</div></div>","PeriodicalId":13854,"journal":{"name":"International Dairy Journal","volume":"177 ","pages":"Article 106586"},"PeriodicalIF":3.4,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146172906","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A brief history of casein micelles: On the origin of models","authors":"Skelte G. Anema","doi":"10.1016/j.idairyj.2026.106598","DOIUrl":"10.1016/j.idairyj.2026.106598","url":null,"abstract":"<div><div>The casein micelles are colloidal particles found in the milk of mammalian species. They contain caseins coupled with milk salts, in particular calcium and phosphate. Although intensely studied, the structure of the casein micelles in bovine milk is not known with certainty, although numerous models have been proposed. This review on casein micelle structural models is divided into two sections. The first section provides a historical review of the key pieces of information about caseins and casein micelles that was required in order to propose models for the casein micelle structure. The second section sequentially reviews the models of the casein micelles from the first structure proposed in 1958 to those of the present day. A final section is included, which gives a brief opinion as to whether we are at a consensus on the structure of the casein micelles, and whether the latest models adequately explain the properties of the natural casein micelles in milk.</div></div>","PeriodicalId":13854,"journal":{"name":"International Dairy Journal","volume":"177 ","pages":"Article 106598"},"PeriodicalIF":3.4,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147386472","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Emerging strategies for monitoring and mitigating Pseudomonas species contamination in milk and dairy food","authors":"Yan Qi,&nbsp;Chunping You","doi":"10.1016/j.idairyj.2026.106596","DOIUrl":"10.1016/j.idairyj.2026.106596","url":null,"abstract":"<div><div>Milk and dairy products are valued for their nutrition, making high quality a common pursuit for dairy producers and consumers. <em>Pseudomonas</em> spp. are prevalent during dairy processing and can thrive under cold temperatures, posing a latent risk for cold chain storage and transportation. Although thermal treatment effectively inactivates <em>Pseudomonas</em> cells, their secreted enzymes remain active even after ultra-high temperature processing, hydrolyzing dairy components and causing spoilage. This review summarizes the major <em>Pseudomonas</em> species and their protease. It also evaluates rapid detection methods (e.g., PCR, isothermal amplification) and technologies for controlling microbial load (e.g., essential oils, bacteriophages). Furthermore, bacterial typing for contamination source tracking is discussed. Also, the challenges and future prospective are proposed with the aim of advancing practical applications in dairy field. This review will facilitate a thorough understanding of <em>Pseudomonas</em> spp. and outline effective strategies to ensure the quality and safety of milk and dairy products.</div></div>","PeriodicalId":13854,"journal":{"name":"International Dairy Journal","volume":"177 ","pages":"Article 106596"},"PeriodicalIF":3.4,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147386502","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bioactive peptides from whey proteins: production, purification, identification, mechanism of action and biofunctionality in foods","authors":"Aliou Toro Lafia ,&nbsp;Winston Pinheiro Claro Gomes ,&nbsp;Wanessa R. Melchert","doi":"10.1016/j.idairyj.2026.106595","DOIUrl":"10.1016/j.idairyj.2026.106595","url":null,"abstract":"<div><div>Bioactive peptides are specific protein fragments capable of exerting relevant biological activities. In recent years, agro-industrial by-products, such as whey, have been widely explored as sustainable protein sources for the production of these compounds. This narrative review provides an integrated overview of recent advances in the production, extraction, purification, and identification of bioactive peptides derived from whey proteins, with emphasis on their potential applications as antioxidant, antimicrobial, and functional food ingredients. The mechanisms of action underlying the antioxidant and antimicrobial activities of these peptides are also addressed. Enzymatic hydrolysis is the primary strategy for obtaining bioactive peptides due to its efficiency in releasing biologically active sequences; however, exploration of emerging physical technologies remains limited. Chromatographic techniques for the purification, fractionation, and isolation of peptides with defined bioactivities have undergone significant technological advances, ranging from conventional liquid chromatography to ultra-high-performance liquid chromatography (UHPLC). Peptide sequencing and identification are primarily performed using liquid chromatography coupled with mass spectrometry. These processes have also seen significant technological advances with the development of more efficient ionization sources and mass analyzers, such as quadrupole (Q), time-of-flight (TOF), and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF), often coupled to UHPLC systems. Antioxidant peptides act mainly through free radical scavenging and the chelation of pro-oxidant metals, whereas antimicrobial peptides exert their effects by inhibiting essential extracellular and intracellular structures of microorganisms. In this context, whey-derived bioactive peptides are promising alternatives for food preservation and functional food development.</div></div>","PeriodicalId":13854,"journal":{"name":"International Dairy Journal","volume":"177 ","pages":"Article 106595"},"PeriodicalIF":3.4,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147386503","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Influence of protein concentration, pH, and calcium sequestering salts on rehydration and physicochemical properties of casein-based powders recovered from expired pasteurized milk","authors":"Hooriyeh Mohammadpour ,&nbsp;Luisa Pellegrino ,&nbsp;Marta Sindaco ,&nbsp;Stefano Cattaneo ,&nbsp;Veronica Rosi ,&nbsp;Thom Huppertz ,&nbsp;Paolo D'Incecco","doi":"10.1016/j.idairyj.2026.106604","DOIUrl":"10.1016/j.idairyj.2026.106604","url":null,"abstract":"<div><div>Acid casein, sodium caseinate, co-precipitate, and rennet casein were prepared from expired pasteurized milk. The effects of two calcium sequestering salts, trisodium citrate (TSC) and disodium phosphate (DSP) and two pH values (unchanged and 9) were evaluated upon solubilization of casein-based powders. The powders were first dispersed in 30 mmol L⁻¹ TSC and heated at 60 °C for 45 min. Due to their poor solubility, rennet casein and co-precipitate were further examined in 112 mmol L⁻¹ DSP. Dispersions were characterized for particle size distribution and microstructure. Selected combinations of explored conditions caused an improved solubility but were not enough effective in dissociating the para-casein network of rennet casein. Capillary zone electrophoresis of the insoluble material indicated the preferential solubilization of modified, presumably glycated, caseins. This study provides new findings on the behaviour of casein powders recovered from expired pasteurized milk, thus contributing to implementation of strategies for food waste valorisation.</div></div>","PeriodicalId":13854,"journal":{"name":"International Dairy Journal","volume":"177 ","pages":"Article 106604"},"PeriodicalIF":3.4,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147386505","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}