{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T20:28:17Z","timestamp":1787776097232,"version":"build-2784847793"},"reference-count":41,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"8","license":[{"start":{"date-parts":[[2025,8,1]],"date-time":"2025-08-01T00:00:00Z","timestamp":1754006400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-sa\/4.0"}],"content-domain":{"domain":["lww.com","ovid.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2025,8]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Aim:<\/jats:title>\n                    <jats:p>\n                      This study aimed to formulate a protocol to isolate and characterize immunoglobulin Y (IgY) antibodies from chicken egg yolk and evaluate its potential in inhibiting\n                      <jats:italic toggle=\"yes\">Streptococcus mutans<\/jats:italic>\n                      .\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Materials and Methods:<\/jats:title>\n                    <jats:p>\n                      Part A: IgY was extracted from fresh chicken egg yolk using a polyethylene glycol precipitation method. The isolated IgY was characterized using ultraviolet-visible (UV-Vis) spectroscopy to assess protein concentration and purity, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for molecular weight confirmation, high-performance liquid chromatography (HPLC) for purity, and mass spectrometry for further protein analysis. Functional activity was evaluated using Western blotting and enzyme-linked immunosorbent assay (ELISA) to confirm antigen binding. PART B: antimicrobial testing: (i) minimum inhibitory concentration (MIC) assays: determining the lowest concentration of IgY that inhibits the growth of each pathogen and (ii) zone of inhibition tests: measuring the effectiveness of IgY in inhibiting pathogen growth on agar plates. The concentration of IgY 50 \u03bcl, and 100 \u03bcl was utilized against\n                      <jats:italic toggle=\"yes\">S. mutans<\/jats:italic>\n                      ,\n                      <jats:italic toggle=\"yes\">Enterococcus faecalis<\/jats:italic>\n                      , and\n                      <jats:italic toggle=\"yes\">Candida albicans<\/jats:italic>\n                      .\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results:<\/jats:title>\n                    <jats:p>\n                      The UV-Vis spectroscopy results indicated a high concentration of IgY with minimal impurities. SDS-PAGE revealed a single band at approximately 180 kDa, corresponding to the expected molecular weight of IgY, with no significant contamination. HPLC analysis confirmed a pure IgY preparation with a single major peak. Mass spectrometry further validated the molecular weight of the IgY at ~180 kDa. Functional assays (western blotting and ELISA) demonstrated that the isolated IgY retained its ability to bind specifically to\n                      <jats:italic toggle=\"yes\">S. mutans<\/jats:italic>\n                      , confirming its potential as an antimicrobial agent. MIC assays showed that IgY effectively inhibited the growth of endodontic pathogens at relatively low concentrations. The zone of inhibition for\n                      <jats:italic toggle=\"yes\">S. mutans<\/jats:italic>\n                      group was as follows: positive control (PC) - 13 mm, test-50 \u03bcL - 11 mm, and test 100 \u03bcL - 20 mm; for\n                      <jats:italic toggle=\"yes\">E. faecalis<\/jats:italic>\n                      \u2013 50 \u03bcL - 14 mm, 50 \u03bcL - 15 mm, and PC - 15 mm; for\n                      <jats:italic toggle=\"yes\">C. albicans<\/jats:italic>\n                      \u2013 100 \u03bcL - 26 mm 100 \u03bcL - 24 mm and PC - 18 mm.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion:<\/jats:title>\n                    <jats:p>\n                      IgY antibodies isolated from chicken egg yolk were characterized as highly pure and functional, with a strong potential for use in inhibiting\n                      <jats:italic toggle=\"yes\">S. mutans<\/jats:italic>\n                      \u2013 an established dental caries causative microorganism. The use of IgY could offer an effective, ethical, and cost-efficient alternative to mammalian antibodies in oral health treatments, particularly for targeting\n                      <jats:italic toggle=\"yes\">S. mutans<\/jats:italic>\n                      , and can be a viable therapeutic tool in passive immunization, caries prevention, and caries inhibition. It also has inhibitory potential on\n                      <jats:italic toggle=\"yes\">E. faecalis<\/jats:italic>\n                      and\n                      <jats:italic toggle=\"yes\">C. albicans<\/jats:italic>\n                      and can be developed as a therapeutic agent in endodontic infections.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.4103\/jcde.jcde_185_25","type":"journal-article","created":{"date-parts":[[2025,8,1]],"date-time":"2025-08-01T12:03:06Z","timestamp":1754049786000},"page":"772-782","update-policy":"https:\/\/doi.org\/10.1097\/lww.0000000000001000","source":"Crossref","is-referenced-by-count":1,"title":["Standardization of extraction, identification, and characterization of an immunoglobulin Y antibody: A potential inhibitor of cariogenic and endodontic microbiome"],"prefix":"10.4103","volume":"28","author":[{"given":"Monisha","family":"Bhate","sequence":"first","affiliation":[{"name":"Department of Conservative Dentistry 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