Probiotics and Antimicrobial Proteins最新文献

{"title":"Human Defensins: Structure, Function, and Potential as Therapeutic Antimicrobial Agents with Highlights Against SARS CoV-2.","authors":"Maryam Nagib, Ahmed M Sayed, Ahmed H Korany, Karim Abdelkader, Falah H Shari, William G Mackay, Mostafa E Rateb","doi":"10.1007/s12602-024-10436-8","DOIUrl":"10.1007/s12602-024-10436-8","url":null,"abstract":"<p><p>The human defensins are a group of cationic antimicrobial peptides that range in size from 2 to 5 kDa and share a common structural motif of six disulphide-linked cysteines. Several naturally occurring human α- and β-defensins have been identified over the past two decades. They have a wide variety of antimicrobial effects, and their potential to avoid the development of resistance to antimicrobial treatment makes them attractive as therapeutic agents. Human defensins have recently been the focus of medical and molecular biology studies due to their promising application in medicine and the pharmaceutical industry. This work aims to provide a comprehensive summary of the current developments of human defensins, including their identification, categorization, molecular features, expression, modes of action, and potential application in medical settings. Current obstacles and future opportunities for using human defensins are also covered. Furthermore, we shed light on the potential of this class as an antiviral agent, particularly against SARS CoV-2, by providing an in silico-based investigation of their plausible mechanisms of action.</p>","PeriodicalId":20506,"journal":{"name":"Probiotics and Antimicrobial Proteins","volume":" ","pages":"1563-1583"},"PeriodicalIF":4.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12055905/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142847480","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lysozyme Peptides as a Novel Nutra-Preservative to Control Some Food Poisoning and Food Spoilage Microorganisms.","authors":"Adham M Abdou, Dina A B Awad","doi":"10.1007/s12602-024-10226-2","DOIUrl":"10.1007/s12602-024-10226-2","url":null,"abstract":"<p><p>Foodborne illnesses and microbial food contamination are crucial concerns and still issues of great worldwide concern. Additionally, the serious health hazards associated with the use of chemical preservatives in food technology. Lysozyme (Lz) is an active protein against Gram-positive bacterial cell wall through its muramidase lytic activity; however, several authors could identify some antimicrobial peptides derived from Lz that have an exaggerated and broad-spectrum antibacterial activity. Therefore, a lysozyme peptides preparation (LzP) is developed to broaden the Lz spectrum. In this work, we investigated the potential efficacy of LzP as a novel Nutra-preservative (food origin) agent against some pathogenic and spoilage bacteria. Our results showed that LzP demonstrated only 11% of the lysozyme lytic activity. However, LzP exhibited strong antibacterial activity against Escherichia coli, Salmonella enteritidis, and Pseudomonas species, while Salmonella typhi and Aeromonas hydrophila exhibited slight resistance. Despite the lowest LzP concentration (0.1%) employed, it performs stronger antibacterial activity than weak organic acids (0.3%). Interestingly, the synergistic multi-component formulation (LzP, glycine, and citric acid) could inhibit 6 log₁₀ cfu/ml of E. coli survival growth. The effect of heat treatment on LzP showed a decrease in its antibacterial activity at 5 and 67% by boiling at 100 °C/30 min, and autoclaving at 121 °C/15 min; respectively. On the other hand, LzP acquired stable antibacterial activity at different pH values (4-7). In conclusion, LzP would be an innovative, natural, and food origin preservative to control the growth of food poisoning and spoilage bacteria in food instead chemical one.</p>","PeriodicalId":20506,"journal":{"name":"Probiotics and Antimicrobial Proteins","volume":" ","pages":"1663-1673"},"PeriodicalIF":4.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12055936/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139906298","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antifungal, Antimycobacterial, Protease and α‒Amylase Inhibitory Activities of a Novel Serine Bifunctional Protease Inhibitor from Adenanthera pavonina L. Seeds.","authors":"Rodrigo da Silva Gebara, Marciele Souza da Silva, Sanderson Dias Calixto, Thatiana Lopes Biá Ventura Simão, Ana Eliza Zeraik, Elena Lassounskaia, Michelle Frazão Muzitano, Jorge Hudson Petretski, Valdirene Moreira Gomes, André de Oliveira Carvalho","doi":"10.1007/s12602-023-10194-z","DOIUrl":"10.1007/s12602-023-10194-z","url":null,"abstract":"<p><p>Antifungal resistance poses a significant challenge to disease management, necessitating the development of novel drugs. Antimicrobial peptides offer potential solutions. This study focused on extraction and characterization of peptides from Adenanthera pavonina seeds with activity against Candida species, Mycobacterium tuberculosis, proteases, and α-amylases. Peptides were extracted in phosphate buffer and heated at 90°C for 10 min to create a peptide rich heated fraction (PRHF). After confirming antimicrobial activity and the presence of peptides, the PRHF underwent ion exchange chromatography, yielding retained and non-retained fractions. These fractions were evaluated for antimicrobial activity and cytotoxicity against murine macrophages. The least toxic and most active fraction underwent reversed-phase chromatography, resulting in ten fractions. These fractions were tested for peptides and antimicrobial activity. The most active fraction was rechromatographed on a reversed-phase column, resulting in two fractions that were assessed for antimicrobial activity. The most active fraction revealed a single band of approximately 6 kDa and was tested for inhibitory effects on proteases and α-amylases. Thermal stability experiments were conducted on the 6 kDa peptide at different temperatures followed by reassessment of antifungal activity and circular dichroism. The 6 kDa peptide inhibited yeasts, M. tuberculosis, human salivary and Tenebrio molitor larvae intestine α-amylases, and proteolytic activity from fungal extracts, and thus named ApPI. Remarkably, ApPI retained antifungal activity and conformation after heating and is primarily composed of α-helices. ApPI is a thermally stable serine protease/α-amylase inhibitor from A. pavonina seeds, offering promise as a foundational molecule for innovative therapeutic agents against fungal infections and tuberculosis.</p>","PeriodicalId":20506,"journal":{"name":"Probiotics and Antimicrobial Proteins","volume":" ","pages":"1320-1342"},"PeriodicalIF":4.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138804374","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bacillus subtilis Induces Human Beta Defensin-2 Through its Lipoproteins in Human Intestinal Epithelial Cells.","authors":"Yoon Ju So, Ok-Jin Park, Yeongkag Kwon, Jintaek Im, Dongwook Lee, Sung-Ho Yun, Kun Cho, Cheol-Heui Yun, Seung Hyun Han","doi":"10.1007/s12602-024-10224-4","DOIUrl":"10.1007/s12602-024-10224-4","url":null,"abstract":"<p><p>Human intestinal epithelial cells (IECs) play an important role in maintaining gut homeostasis by producing antimicrobial peptides (AMPs). Bacillus subtilis, a commensal bacterium, is considered a probiotic. Although its protective effects on intestinal health are widely reported, the key component of B. subtilis responsible for its beneficial effects remains elusive. In this study, we tried to identify the key molecules responsible for B. subtilis-induced AMPs and their molecular mechanisms in a human IEC line, Caco-2. B. subtilis increased human beta defensin (HBD)-2 mRNA expression in a dose- and time-dependent manner. Among the B. subtilis microbe-associated molecular patterns, lipoprotein (LPP) substantially increased the mRNA expression and protein production of HBD-2, whereas lipoteichoic acid and peptidoglycan did not show such effects. Those results were confirmed in primary human IECs. In addition, both LPP recognition and HBD-2 secretion mainly took place on the apical side of fully differentiated and polarized Caco-2 cells through Toll-like receptor 2-mediated JNK/p38 MAP kinase/AP-1 and NF-κB pathways. HBD-2 efficiently inhibited the growth of the intestinal pathogens Staphylococcus aureus and Bacillus cereus. Furthermore, LPPs pre-incubated with lipase or proteinase K decreased LPP-induced HBD-2 expression, suggesting that the lipid and protein moieties of LPP are crucial for HBD-2 expression. Q Exactive Plus mass spectrometry identified 35 B. subtilis LPP candidates within the LPP preparation, and most of them were ABC transporters. Taken together, these results suggest that B. subtilis promotes HBD-2 secretion in human IECs mainly with its LPPs, which might enhance the protection from intestinal pathogens.</p>","PeriodicalId":20506,"journal":{"name":"Probiotics and Antimicrobial Proteins","volume":" ","pages":"1648-1662"},"PeriodicalIF":4.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12055916/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139906296","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Multi-Enzyme Supplementation to Diets Containing 2 Protein Levels Affects Intramuscular Fat Content in Muscle and Modulates Cecal Microflora Without Affecting the Growth Performance of Finishing Pigs.","authors":"Qianqian Zhang, Sungbo Cho, Junho Song, Jinuk Jeong, Minjae Yu, Seyoung Mun, Kyudong Han, In Ho Kim","doi":"10.1007/s12602-023-10169-0","DOIUrl":"10.1007/s12602-023-10169-0","url":null,"abstract":"<p><p>We investigated the effects of crude protein (CP) levels and exogenous enzymes on growth performance, meat quality, toxic gas emissions, and colonic microbiota community in 200 finishing pigs. Four groups corresponded to 4 diets: 16.74% CP (high-protein level, HP) and 14.73% CP (medium protein level, MP) diet supplemented with or without 1-g/kg multi-enzymes (ENZs, including 1000-U/kg protease, 2500-U/kg α-amylase, and 10,000-U/kg β-glucanase), using a 2 × 2 factorial arrangement. After 7 weeks of trial, ENZs supplementation increased (P < 0.05) the average daily gain (ADG) of finishing pigs during weeks 4 to 7 and in the overall period and improved gross energy utilization. Dietary HP improved (P < 0.05) ADG during the overall period. The MP diet-treated pigs had higher intramuscular fat (IMF) content in the longissimus dorsi muscle (P < 0.01). ENZs supplementation to the MP diets lowered muscle IMF content (P < 0.01). Additionally, pigs fed the HP diet released (P < 0.05) more NH₃ and H₂S in excrement. The HP diet enhanced (P < 0.05) intestinal microbial richness, represented by higher observed_ amplicon sequence variants and Chao1. Administration of ENZs to the HP diet increased (P < 0.05) the Shannon and Pielou's evenness. Dietary MP promoted Firmicutes proliferation. Supplementary HP diet increased the relative abundances of Spirochaetota, Verrucomicrobiota, Desulfobacterota, and Fibrobacterota (P < 0.05). Supplemental ENZ elevated (P < 0.05) Actinobacteriota and Desulfobacterota abundances. ENZ supplementation to the HP diet increased the abundances of Bacteroidota, Desulfobacterota, and Proteobacteria but lowered their abundances in the MP diet. Taken together, the HP diet or ENZs' supplements improved growth performance. Although the interaction between CP levels and ENZs had no effect on growth performance, it modulated colonic flora and muscle IMF content.</p>","PeriodicalId":20506,"journal":{"name":"Probiotics and Antimicrobial Proteins","volume":" ","pages":"976-990"},"PeriodicalIF":4.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41169220","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Probiotics Encapsulated via Biological Macromolecule for Neurological Therapy and Functional Food: A Review.","authors":"Xitong Wang, Jinhua Hu, Hanzhong Zhang, Peng Zhou","doi":"10.1007/s12602-025-10453-1","DOIUrl":"10.1007/s12602-025-10453-1","url":null,"abstract":"<p><p>Probiotics are live microorganisms that confer health benefits to humans, offering significant potential for preventing and treating various diseases. Neurological disorders, driven by multifaceted factors and linked to high disability rates, have become a growing global concern, particularly in the context of an aging population. Recent studies emphasize a strong connection between dysbiosis of the gut microbiota and neurological disorders. Probiotics have emerged as promising therapeutic interventions due to their ability to modulate the gut microbiota and influence the production of key metabolites, such as short-chain fatty acids and neurotransmitters, crucial for neurological health. However, probiotic viability is often compromised, limiting their therapeutic efficacy. We propose that developing high-activity probiotic formulations, coupled with innovative delivery strategies, holds considerable promise for advancing neurological treatments. Encapsulation systems have proven effective in enhancing probiotic stability and efficacy. This review discusses advances in probiotic delivery using biological macromolecule-based encapsulation, addressing key challenges in maintaining viability during production, storage, and digestion. It also highlights emerging delivery systems, such as microencapsulation, aimed at improving stability and therapeutic effectiveness. Additionally, the review explores the potential of functional foods enriched with probiotics for neurological health. Future research should explore clinical applications of encapsulated probiotics and support the development of functional foods to enhance neurological health.</p>","PeriodicalId":20506,"journal":{"name":"Probiotics and Antimicrobial Proteins","volume":" ","pages":"1754-1768"},"PeriodicalIF":4.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143010365","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"New Frontiers in Fighting Mycobacterial Infections: Venom-Derived Peptides.","authors":"Hamed Memariani, Mojtaba Memariani","doi":"10.1007/s12602-025-10455-z","DOIUrl":"10.1007/s12602-025-10455-z","url":null,"abstract":"<p><p>Notwithstanding the indefatigable endeavors to develop effective anti-mycobacterial therapies, mycobacterial infections still present a tough problem for medicine today. The problem is further complicated by the disquieting surge of drug-resistant mycobacterial pathogens, which considerably narrows the existing therapeutic options. Thus, there is a genuine need to discover novel anti-mycobacterial drugs. Animal venoms are considered a treasure trove of structurally variable and biologically active peptides, which may hold promise for therapeutic applications. Over the past two decades, abundant evidence has been amassed regarding anti-mycobacterial effects of various peptides derived from the venoms of honeybees, wasps, scorpions, pseudoscorpions, cone snails, and snakes. This review intends to consolidate the state-of-the-art knowledge on the anti-mycobacterial peptides of animal venoms and to sketch potentially fruitful directions for future investigations. The available data indicate that micromolar concentrations of particular venom-derived peptides can effectively inhibit the in vitro growth of Mycobacterium tuberculosis and non-tuberculous mycobacteria. The proposed mechanisms of action of venom-derived peptides include reduced activity of plasma membrane ATPase, depolarization of the cell membrane, disruption of the cell wall, and increased generation of reactive oxygen species. Interestingly, administering certain peptides (≤ 2 mg/kg body weight) through daily intraperitoneal injections to mice for 8 consecutive days resulted in lower levels of mycobacterial infections and inflammation, hitting two targets with one arrow. Indubitably, such peptides can usher in new possibilities for the prevention and treatment of recalcitrant mycobacterial infections.</p>","PeriodicalId":20506,"journal":{"name":"Probiotics and Antimicrobial Proteins","volume":" ","pages":"1217-1235"},"PeriodicalIF":4.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143010424","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Safety Assessment of Levilactobacillus brevis KU15006: A Comprehensive Analysis of its Phenotypic and Genotypic Properties.","authors":"Min-Gyu Lee, Min-Joo Kang, Suin Kim, Huijin Jeong, Dae-Kyung Kang, Hyun-Dong Paik, Young-Seo Park","doi":"10.1007/s12602-024-10237-z","DOIUrl":"10.1007/s12602-024-10237-z","url":null,"abstract":"<p><p>Levilactobacillus brevis KU15006, isolated from kimchi, exhibits pathogen-antagonistic and anti-diabetic activities; however, the safety of this strain has not been assessed. In the present study, L. brevis KU15006 was evaluated to elucidate its safety as a probiotic strain using phenotypic and genotypic analyses. Its safety was assessed using a minimum inhibitory concentration test comprising nine antibiotics, 26 antibiotic resistance genes, a single conjugative element, virulence gene analysis, hemolysis, cell cytotoxicity, mucin degradation, and toxic metabolite production. L. brevis KU15006 exhibited equal or lower minimum inhibitory concentration for the nine antibiotics than the cut-off value established by the European Food Safety Authority. It did not harbor antibiotic resistance and virulence genes. L. brevis KU15006 lacked β-hemolysis, mucin degradation, cytotoxicity against Caco-2 cells, gelatin liquefaction, bile salt deconjugation, and toxic metabolite production abilities. Based on the results, L. brevis KU15006, which has antagonistic and anti-diabetic effects, could be marketed as a probiotic in the future.</p>","PeriodicalId":20506,"journal":{"name":"Probiotics and Antimicrobial Proteins","volume":" ","pages":"1117-1131"},"PeriodicalIF":4.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140013229","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular Dynamic Study on the Structure and Thermal Stability of Mutant Pediocin PA-1 Peptides Engineered with Cysteine Substitutions.","authors":"Büşra Sevim, Evrim Güneş Altuntaş","doi":"10.1007/s12602-024-10225-3","DOIUrl":"10.1007/s12602-024-10225-3","url":null,"abstract":"<p><p>Pediocin and analogous bacteriocins, valued for thermal stability, serve as versatile antimicrobials in the food sector. Improving their resilience at high temperatures and deriving derivatives not only benefit food production but also offer broad-spectrum antimicrobial potential in pharmaceuticals, spanning treatments for peptic ulcers, women's health, and novel anticancer agents. The study aims to create mutant peptides capable of establishing a third disulfide bond or enhanced through cysteine substitutions. This involves introducing additional Cys residues into the inherent structure of pediocin PA-1 to facilitate disulfide bond formation. Five mutants (Mut 1-5) were systematically generated with double Cys substitutions and assessed for thermal stability through MD simulations across temperatures (298-394 K). The most robust mutants (Mut 1, Mut 4-5) underwent extended analysis via MD simulations, comparing their structural stability, secondary structure, and surface accessibility to the reference Pediocin PA-1 molecule. This comprehensive assessment aims to understand how Cys substitutions influence disulfide bonds and the overall thermal stability of the mutant peptides. In silico analysis indicated that Mut 1 and Mut 5, along with the reference structure, lose their helical structure and one natural disulfide bond at high temperatures, and may impacting antimicrobial activity. Conversely, Mut 4 retained its helical structure and exhibited thermal stability similar to Pediocin PA-1. Pending further experimental validation, this study implies Mut 4 may have high stability and exceptional resistance to high temperatures, potentially serving as an effective antimicrobial alternative.</p>","PeriodicalId":20506,"journal":{"name":"Probiotics and Antimicrobial Proteins","volume":" ","pages":"1739-1753"},"PeriodicalIF":4.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12055943/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139997257","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Improved Bacterial Survival and Antioxidant Activity After In Vitro Digestion of Fermented Dairy Beverages by Lacticaseibacillus casei LC-01 and Lactiplantibacillus plantarum BG-112 Containing Yacon.","authors":"Bruna C A Plank, Karla B Guergoletto, Thais S Rocha","doi":"10.1007/s12602-024-10220-8","DOIUrl":"10.1007/s12602-024-10220-8","url":null,"abstract":"<p><p>The fermentation of milk containing 0%, 3%, 6%, and 9% (w/v) yacon root flour (YRF) by Lacticaseibacillus casei LC-1 and Lactiplantibacillus plantarum BG-112 was evaluated for bacterial survival and antioxidant activity (AA) before and after simulated gastrointestinal digestion. After 28 days of refrigerated storage, samples of the beverages were analyzed for cell viability, AA (using ferric ion reducing antioxidant power (FRAP) and (ABTS), and molecular mass profile of proteins (using electrophoresis). The presence of 9% YRF increased bacterial survival during 28 days of storage and passage through the gastrointestinal tract for both L. casei and L. plantarum, which showed a greater capacity to reduce ferric ions compared to 0% YRF, and the ability to capture free radicals increased from below 5 mM to over 15 mM TE after digestion. Milk proteins are hydrolyzed during digestion, and the generation of bioactive peptides with AA may explain the increase in AA levels. Since peptides are generated from milk proteins, YRF did not influence AA after digestion. These results showed that fermentation of milk by L. casei and L. plantarum with YRF increased the chances of these bacteria reaching the colon in adequate quantities. After simulated digestion, the beverages showed improved AA due to milk protein hydrolysis.</p>","PeriodicalId":20506,"journal":{"name":"Probiotics and Antimicrobial Proteins","volume":" ","pages":"1584-1595"},"PeriodicalIF":4.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139703267","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}