{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T14:07:55Z","timestamp":1789567675074,"version":"build-2803163510"},"reference-count":54,"publisher":"American Chemical Society (ACS)","issue":"36","license":[{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/501100013290","name":"National Key Research and Development Program of China Stem Cell and Translational Research","doi-asserted-by":"publisher","award":["2025YFD1700900"],"award-info":[{"award-number":["2025YFD1700900"]}],"id":[{"id":"10.13039\/501100013290","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007129","name":"Natural Science Foundation of Shandong Province","doi-asserted-by":"publisher","award":["2024HWYQ-012"],"award-info":[{"award-number":["2024HWYQ-012"]}],"id":[{"id":"10.13039\/501100007129","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,16]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Dye-decolorizing peroxidases (DyPs) are promising biocatalysts for lignin valorization and environmental remediation. Here, 427 putative marine Class P DyPs containing the conserved heme-binding motif were retrieved from metagenomic data sets. CatPred and UniKP were used in parallel to rank candidates, while AlphaFold3-derived models served as structural hypotheses for assessing predicted structural diversity and guiding candidate selection. The candidates were grouped into six structural classes, and seven representative enzymes were experimentally examined. Four showed detectable activity, including PhDyP and KpDyP, which exhibited optimal activity at pH 6.0, showed halotolerance, and retained 50% activity at 0 \u00b0C. Comparison of predicted and experimental properties showed that current kinetic-prediction tools support prioritization but do not reliably capture absolute kinetic values, assay-condition effects, heme incorporation, or global structural integrity. These findings expand the characterized diversity of Class P DyPs and support their further exploration as robust enzyme scaffolds for green bioremediation.<\/jats:p>","DOI":"10.1021\/acs.jafc.6c06672","type":"journal-article","created":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T11:40:28Z","timestamp":1788435628000},"page":"28255-28267","source":"Crossref","is-referenced-by-count":0,"title":["AI-Assisted Metagenomic Mining of New Dye-Decolorizing\nPeroxidases: Systematic Biochemical Validation and Catalytic Structural\nDiversity"],"prefix":"10.1021","volume":"74","author":[{"given":"Yitong","family":"Liu","sequence":"first","affiliation":[{"name":"Shandong University , , Binhai Road 72\/N2 , ,","place":["Qingdao, China, 266237"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yixin","family":"Chang","sequence":"additional","affiliation":[{"name":"Shandong University , , Binhai Road 72\/N2 , ,","place":["Qingdao, China, 266237"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yunjia","family":"Guan","sequence":"additional","affiliation":[{"name":"Shandong University , , Binhai Road 72\/N2 , ,","place":["Qingdao, China, 266237"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaoyu","family":"Ma","sequence":"additional","affiliation":[{"name":"Shandong University , , Binhai Road 72\/N2 , ,","place":["Qingdao, China, 266237"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2438-7222","authenticated-orcid":true,"given":"Su","family":"Ma","sequence":"additional","affiliation":[{"name":"Shandong University , , Binhai Road 72\/N2 , ,","place":["Qingdao, China, 266237"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,1]]},"reference":[{"key":"2026091609085489600_cit1","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s10295-013-1371-6","article-title":"DyP-type peroxidases:\na promising\nand versatile class of enzymes","volume":"41","author":"Colpa","year":"2014","journal-title":"J. Ind. Microbiol.\nBiotechnol."},{"key":"2026091609085489600_cit2","doi-asserted-by":"publisher","first-page":"1419","DOI":"10.1007\/s00253-009-2369-x","article-title":"A robust and extracellular heme-containing peroxidase\nfrom Thermobifida fuscaas prototype\nof a bacterial peroxidase superfamily","volume":"86","author":"van Bloois","year":"2010","journal-title":"Appl.\nMicrobiol. Biotechnol."},{"key":"2026091609085489600_cit3","doi-asserted-by":"publisher","first-page":"108153","DOI":"10.1016\/j.biotechadv.2023.108153","article-title":"Biocatalysis\nfor biorefineries: The case of dye-decolorizing peroxidases","volume":"65","author":"Silva","year":"2023","journal-title":"Biotechnol. Adv."},{"key":"2026091609085489600_cit4","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1016\/j.molcatb.2013.09.025","article-title":"Phenol oxidation\nby DyP-type peroxidases in comparison to fungal and plant peroxidases","volume":"103","author":"Liers","year":"2014","journal-title":"J. Mol. Catal. B: Enzym."},{"issue":"13","key":"2026091609085489600_cit5","doi-asserted-by":"publisher","first-page":"5839","DOI":"10.1007\/s00253-012-4521-2","article-title":"Substrate oxidation\nby dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading\nagaricomycetes compared to other fungal and plant heme-peroxidases","volume":"97","author":"Liers","year":"2013","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"2026091609085489600_cit7","doi-asserted-by":"publisher","first-page":"871","DOI":"10.1007\/s00253-010-2633-0","article-title":"New and classic\nfamilies of secreted fungal heme peroxidases","volume":"87","author":"Hofrichter","year":"2010","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"2026091609085489600_cit8","doi-asserted-by":"publisher","first-page":"101401","DOI":"10.1016\/j.bbrep.2022.101401","article-title":"Unexpected diversity of dye-decolorizing\nperoxidases","volume":"33","author":"Yoshida","year":"2023","journal-title":"Biochem. Biophys. Rep."},{"key":"2026091609085489600_cit9","doi-asserted-by":"publisher","first-page":"123136","DOI":"10.1016\/j.ijbiomac.2023.123136","article-title":"Marine enzymes: Classification\nand application in various\nindustries","volume":"230","author":"Ghattavi","year":"2023","journal-title":"Int. J. Biol. Macromol."},{"key":"2026091609085489600_cit10","doi-asserted-by":"publisher","first-page":"5556","DOI":"10.3390\/ijms22168683","article-title":"Characterization of\nclass V DyP-type peroxidase SaDyP1 from Streptomyces avermitilis and evaluation of SaDyPs expression\nin Mycelium","volume":"22","author":"Sugawara","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"2026091609085489600_cit11","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1002\/prot.21550","article-title":"Crystal structures of two novel dye-decolorizing\nperoxidases reveal a \u03b2-barrel fold with a conserved heme-binding\nmotif","volume":"69","author":"Zubieta","year":"2007","journal-title":"Proteins"},{"key":"2026091609085489600_cit12","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/j.abb.2014.12.022","article-title":"Characterisation of Dyp-type peroxidases from Pseudomonas fluorescens Pf-5: Oxidation of Mn(II) and polymeric\nlignin by Dyp1B","volume":"574","author":"Rahmanpour","year":"2015","journal-title":"Arch. Biochem. Biophys."},{"key":"2026091609085489600_cit13","doi-asserted-by":"publisher","first-page":"1387","DOI":"10.1007\/s00018-008-8651-8","article-title":"DyP-type peroxidases\ncomprise a novel heme peroxidase family","volume":"66","author":"Sugano","year":"2009","journal-title":"Cell.\nMol. Life Sci."},{"key":"2026091609085489600_cit14","doi-asserted-by":"publisher","first-page":"3899","DOI":"10.1016\/j.csbj.2022.07.032","article-title":"Unveiling molecular\ndetails behind improved\nactivity at neutral to alkaline pH of an engineered DyP-type peroxidase","volume":"20","author":"Borges","year":"2022","journal-title":"Comput. Struct. Biotechnol. J."},{"key":"2026091609085489600_cit15","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1016\/j.bbrc.2017.01.081","article-title":"Crystal structure and biochemical\nfeatures of dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp 143 and Arg 232 play divergent roles toward\ndifferent substrates","volume":"484","author":"Liu","year":"2017","journal-title":"Biochem. Biophys. Res.\nCommun."},{"key":"2026091609085489600_cit16","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1042\/BJ20141211","article-title":"Catalytic surface radical\nin dye-decolorizing peroxidase: a computational, spectroscopic and\nsite-directed mutagenesis study","volume":"466","author":"Linde","year":"2015","journal-title":"Biochem. J."},{"key":"2026091609085489600_cit17","doi-asserted-by":"publisher","first-page":"34767","DOI":"10.1074\/jbc.M113.514521","article-title":"Structural basis of substrate conversion\nin a new aromatic peroxygenase: cytochrome P450 functionality with\nbenefits","volume":"288","author":"Piontek","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2026091609085489600_cit18","doi-asserted-by":"publisher","first-page":"743","DOI":"10.1007\/s00775-021-01896-2","article-title":"Aspartate or arginine? Validated redox state X-ray\nstructures elucidate mechanistic subtleties of FeIV = O formation\nin bacterial dye-decolorizing peroxidases","volume":"26","author":"Luc\u030cic\u0301","year":"2021","journal-title":"J.\nBiol. Inorg. Chem."},{"key":"2026091609085489600_cit19","doi-asserted-by":"publisher","first-page":"478","DOI":"10.3390\/md9040478","article-title":"Marine biocatalysts:\nenzymatic features and applications","volume":"9","author":"Trincone","year":"2011","journal-title":"Mar. Drugs"},{"key":"2026091609085489600_cit20","doi-asserted-by":"publisher","first-page":"1299","DOI":"10.1007\/s12010-020-03483-8","article-title":"Marine bacterial\nesterases: a comprehensive review","volume":"164","author":"Barzkar","year":"2020","journal-title":"Int. J. Biol.\nMacromol."},{"key":"2026091609085489600_cit21","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1186\/1475-2859-7-27","article-title":"Marine\nmetagenomics: strategies for\nthe discovery of novel enzymes with biotechnological applications\nfrom marine environments","volume":"7","author":"Kennedy","year":"2008","journal-title":"Microb. Cell Fact."},{"key":"2026091609085489600_cit22","first-page":"6275","article-title":"Machine learning-based\nprediction of enzyme substrate specificity and its application to\nDyP peroxidase","volume":"60","author":"Suda","year":"2020","journal-title":"J. Chem. Inf. Model."},{"key":"2026091609085489600_cit23","doi-asserted-by":"publisher","first-page":"5556","DOI":"10.3390\/ijms22115556","article-title":"DyP-Type peroxidases:\nrecent advances and perspectives","volume":"22","author":"Sugano","year":"2021","journal-title":"Int. J. Mol.\nSci."},{"key":"2026091609085489600_cit24","doi-asserted-by":"publisher","first-page":"2072","DOI":"10.1038\/s41467-025-57215-9","article-title":"CatPred: a comprehensive\nframework for deep learning\nin vitro enzyme kinetic parameters","volume":"16","author":"Boorla","year":"2025","journal-title":"Nat. Commun."},{"key":"2026091609085489600_cit25","doi-asserted-by":"publisher","first-page":"8211","DOI":"10.1038\/s41467-023-44113-1","article-title":"UniKP: a unified\nframework for the prediction of enzyme kinetic parameters","volume":"14","author":"Yu","year":"2023","journal-title":"Nat. Commun."},{"key":"2026091609085489600_cit26","doi-asserted-by":"publisher","first-page":"371","DOI":"10.1038\/s41586-024-07891-2","article-title":"Global marine microbial\ndiversity and its potential in bioprospecting","volume":"633","author":"Chen","year":"2024","journal-title":"Nature"},{"key":"2026091609085489600_cit27","doi-asserted-by":"publisher","first-page":"0153","DOI":"10.34133\/research.0153","article-title":"Enzyme\ncommission number prediction and benchmarking with hierarchical\ndual-core multitask learning framework","volume":"6","author":"Shi","year":"2023","journal-title":"Research"},{"key":"2026091609085489600_cit28","doi-asserted-by":"publisher","first-page":"2417","DOI":"10.1111\/jam.15707","article-title":"Characterization\nof three novel DyP-type peroxidases from Streptomyces chartreusis NRRL 3882","volume":"133","author":"Yayci","year":"2022","journal-title":"J. Appl. Microbiol."},{"key":"2026091609085489600_cit29","doi-asserted-by":"publisher","first-page":"111651","DOI":"10.1016\/j.jinorgbio.2021.111651","article-title":"Discovery and characterization\nof a novel Dyp-type peroxidase from\na marine actinobacterium isolated from Trondheim fjord, Norway","volume":"226","author":"Cordas","year":"2022","journal-title":"J. Inorg. Biochem."},{"key":"2026091609085489600_cit30","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1186\/s43141-020-00043-9","article-title":"Metagenomic applications in exploration and development of novel\nenzymes from nature: a review","volume":"18","author":"Prayogo","year":"2020","journal-title":"J. Genet. Eng.\nBiotechnol."},{"key":"2026091609085489600_cit31","doi-asserted-by":"publisher","first-page":"1969","DOI":"10.1038\/s41598-018-36950-8","article-title":"Web-based\ndisplay of protein surface and pH-dependent\nproperties for assessing the developability of biotherapeutics","volume":"9","author":"Hebditch","year":"2019","journal-title":"Sci. Rep."},{"key":"2026091609085489600_cit32","doi-asserted-by":"publisher","first-page":"716","DOI":"10.1038\/s42256-025-01026-6","article-title":"Machine learning prediction\nof enzyme optimum pH","volume":"7","author":"Gado","year":"2025","journal-title":"Nat. Mach. Intell."},{"key":"2026091609085489600_cit33","doi-asserted-by":"publisher","first-page":"92","DOI":"10.1186\/s13059-026-03986-3","article-title":"A geometric\ndeep learning framework for genome-wide prediction of enzyme turnover\nnumber","volume":"27","author":"Pan","year":"2026","journal-title":"Genome Biol."},{"key":"2026091609085489600_cit34","doi-asserted-by":"publisher","first-page":"bbag002","DOI":"10.1093\/bib\/bbag002","article-title":"Machine learning\nfor enzyme catalytic activity: current progress and future horizons","volume":"27","author":"Qiu","year":"2026","journal-title":"Brief Bioinform."},{"key":"2026091609085489600_cit35","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/j.abb.2015.03.009","article-title":"An integrated view of\nredox and catalytic properties of B-type PpDyP from Pseudomonas putida MET94 and\nits distal variants","volume":"574","author":"Mendes","year":"2015","journal-title":"Arch. Biochem. Biophys."},{"key":"2026091609085489600_cit36","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","article-title":"Accurate structure prediction\nof biomolecular interactions with AlphaFold\n3","volume":"630","author":"Abramson","year":"2024","journal-title":"Nature"},{"key":"2026091609085489600_cit37","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1038\/s41564-025-02237-8","article-title":"Cell cycle dysregulation of globally important SAR11\nbacteria resulting\nfrom environmental perturbation","volume":"11","author":"Cheng","year":"2026","journal-title":"Nat. Microbiol."},{"key":"2026091609085489600_cit38","doi-asserted-by":"publisher","first-page":"1553","DOI":"10.1038\/ismej.2014.60","article-title":"Implications of streamlining theory\nfor microbial ecology","volume":"8","author":"Giovannoni","year":"2014","journal-title":"ISME J."},{"key":"2026091609085489600_cit39","first-page":"1269","article-title":"Analyse\nspectrale: Sur le spectre d\u2019absorption du sang dans la partie\nviolette et ultra-violette","volume":"97","author":"Soret","year":"1883","journal-title":"C. R. Acad. Sci."},{"key":"2026091609085489600_cit40","doi-asserted-by":"publisher","first-page":"775","DOI":"10.1021\/acs.jcim.1c01315","article-title":"Global analysis of\nheme proteins\nelucidates the correlation between heme distortion and the heme-binding\npocket","volume":"62","author":"Kondo","year":"2022","journal-title":"J. Chem. Inf. Model."},{"key":"2026091609085489600_cit41","doi-asserted-by":"publisher","first-page":"3844","DOI":"10.1021\/acs.jpcb.6b01497","article-title":"Measurement\nof Heme Ruffling Changes\nin MhuD Using UV\u2013vis Spectroscopy","volume":"120","author":"Graves","year":"2016","journal-title":"J.\nPhys. Chem. B"},{"key":"2026091609085489600_cit42","doi-asserted-by":"publisher","first-page":"2053","DOI":"10.1007\/s00253-013-5041-4","article-title":"New dye-decolorizing\nperoxidases from Bacillus subtilis and Pseudomonas putida MET94: towards biotechnological applications","volume":"98","author":"Santos","year":"2014","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"2026091609085489600_cit43","doi-asserted-by":"publisher","first-page":"10579","DOI":"10.1007\/s00253-018-9409-3","article-title":"Characterization and\nuse of a bacterial lignin peroxidase with an improved manganese-oxidative\nactivity","volume":"102","author":"Vignali","year":"2018","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"2026091609085489600_cit44","doi-asserted-by":"publisher","first-page":"3866","DOI":"10.1021\/acsomega.3c07963","article-title":"Dye-decolorizing\nperoxidase of Streptomyces coelicolor (ScDyPB) exists\nas a dynamic mixture of kinetically different oligomers","volume":"9","author":"Pupart","year":"2024","journal-title":"ACS Omega"},{"key":"2026091609085489600_cit45","doi-asserted-by":"publisher","first-page":"141852","DOI":"10.1016\/j.molstruc.2025.141852","article-title":"Exploring enzyme thermostability\nenhancement through molecular modification: What remains to be known?","volume":"1337","author":"Almansoori","year":"2025","journal-title":"J. Mol. Struct."},{"key":"2026091609085489600_cit46","doi-asserted-by":"publisher","first-page":"1152847","DOI":"10.3389\/fmicb.2023.1152847","article-title":"Advances in cold-adapted\nenzymes derived from microorganisms","volume":"14","author":"Liu","year":"2023","journal-title":"Front.\nMicrobiol."},{"key":"2026091609085489600_cit47","unstructured":"Shrestha, R.\n          \n          Molecular mechanism and\nenzymological studies of dye-decolorizing peroxidases (DyPs) from\nThermomonospora curvata and Enterobacter lignolyticus. Ph.D.\nDissertation, Kansas State University, Manhattan, KS, 2017."},{"key":"2026091609085489600_cit48","doi-asserted-by":"publisher","first-page":"5108","DOI":"10.1021\/bi200427h","article-title":"Characterization\nof dye-decolorizing peroxidases from Rhodococcus jostii RHA1","volume":"50","author":"Roberts","year":"2011","journal-title":"Biochemistry"},{"key":"2026091609085489600_cit49","first-page":"857","article-title":"Serial femtosecond zero dose crystallography captures a water-bound\nresting state of a heme enzyme","volume":"7","author":"Luc\u030cic\u0301","year":"2020","journal-title":"IUCrJ."},{"key":"2026091609085489600_cit50","doi-asserted-by":"publisher","first-page":"14823","DOI":"10.1074\/jbc.RA118.004773","article-title":"Roles of distal aspartate\nand arginine of B-class dye-decolorizing\nperoxidase in heterolytic hydrogen peroxide cleavage","volume":"293","author":"Pfanzagl","year":"2018","journal-title":"J. Biol. Chem."},{"key":"2026091609085489600_cit51","doi-asserted-by":"publisher","first-page":"4095","DOI":"10.1074\/jbc.M112.400176","article-title":"First\ncrystal structure\nof a fungal high-redox potential dye-decolorizing peroxidase: substrate\ninteraction sites and long-range electron transfer","volume":"288","author":"Strittmatter","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2026091609085489600_cit52","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1016\/j.abb.2015.03.004","article-title":"Substrate, product, and cofactor: The extraordinarily\nflexible relationship between the CDE superfamily and heme","volume":"574","author":"Celis","year":"2015","journal-title":"Arch. Biochem. Biophys."},{"key":"2026091609085489600_cit53","doi-asserted-by":"publisher","first-page":"2838","DOI":"10.3390\/molecules29122838","article-title":"Three-dimensional\ninteraction homology: deconstructing residue\u2013residue and residue\u2013lipid\ninteractions in membrane proteins","volume":"29","author":"Kellogg","year":"2024","journal-title":"Molecules"},{"key":"2026091609085489600_cit54","doi-asserted-by":"publisher","first-page":"1859","DOI":"10.1002\/jcc.20945","article-title":"CHARMM-GUI: a web-based graphical\nuser interface for CHARMM","volume":"29","author":"Jo","year":"2008","journal-title":"J. Comput. Chem."},{"key":"2026091609085489600_cit55","doi-asserted-by":"publisher","first-page":"3899","DOI":"10.1016\/j.csbj.2022.07.032","article-title":"Unveiling molecular details behind\nimproved activity at neutral to alkaline pH of an engineered DyP-type\nperoxidase","volume":"20","author":"Borges","year":"2022","journal-title":"Comput. Struct. Biotechnol. J."}],"container-title":["Journal of Agricultural and Food Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.jafc.6c06672","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/jafcau\/article-pdf\/74\/36\/28255\/68125057\/acs.jafc.6c06672.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/jafcau\/article-pdf\/74\/36\/28255\/68125057\/acs.jafc.6c06672.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T13:32:27Z","timestamp":1789565547000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/jafcau\/article\/74\/36\/28255\/5397833\/AI-Assisted-Metagenomic-Mining-of-New-Dye"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,1]]},"references-count":54,"journal-issue":{"issue":"36","published-online":{"date-parts":[[2026,9,1]]},"published-print":{"date-parts":[[2026,9,16]]}},"URL":"https:\/\/doi.org\/10.1021\/acs.jafc.6c06672","relation":{},"ISSN":["0021-8561","1520-5118"],"issn-type":[{"value":"0021-8561","type":"print"},{"value":"1520-5118","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,1]]}}}