{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T04:52:23Z","timestamp":1781844743468,"version":"3.54.5"},"reference-count":55,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100003459","name":"Guizhou University","doi-asserted-by":"publisher","award":["[2023] 21"],"award-info":[{"award-number":["[2023] 21"]}],"id":[{"id":"10.13039\/501100003459","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004001","name":"Guizhou Provincial Science and Technology Department","doi-asserted-by":"publisher","award":["2022"],"award-info":[{"award-number":["2022"]}],"id":[{"id":"10.13039\/501100004001","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2026,1]]},"DOI":"10.1016\/j.ijbiomac.2025.148985","type":"journal-article","created":{"date-parts":[[2025,11,14]],"date-time":"2025-11-14T01:27:05Z","timestamp":1763083625000},"page":"148985","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"P1","title":["A novel heat-resistant hydroxycinnamic acid decarboxylase from Wickerhamomyces anomalus"],"prefix":"10.1016","volume":"335","author":[{"given":"Wei","family":"Yang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hexia","family":"Ding","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maodie","family":"Zeng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mai","family":"Cheng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mian","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jianli","family":"Zhou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wangni","family":"Meng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2025.148985_bb0005","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/j.foodchem.2017.10.106","article-title":"Hydroxycinnamic acids loaded in lipid-core nanocapsules","volume":"245","author":"Granata","year":"2018","journal-title":"Food Chem."},{"issue":"2","key":"10.1016\/j.ijbiomac.2025.148985_bb0010","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1007\/s13765-015-0137-4","article-title":"Bacterial synthesis of four hydroxycinnamic acids","volume":"59","author":"An","year":"2016","journal-title":"Appl. Biol. Chem."},{"issue":"4","key":"10.1016\/j.ijbiomac.2025.148985_bb0015","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1016\/S0141-0229(97)00169-5","article-title":"Purification and characterization of hydroxycinnamate decarboxylase from Brettanomyces anomalus","volume":"22","author":"Edlin","year":"1998","journal-title":"Enzyme Microb. Technol."},{"issue":"4","key":"10.1016\/j.ijbiomac.2025.148985_bb0020","doi-asserted-by":"crossref","DOI":"10.3390\/ijms25042075","article-title":"Cloning and characterization of chitin deacetylase from Euphausia superba","volume":"25","author":"Wang","year":"2024","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0025","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.indcrop.2018.02.043","article-title":"Production of vanillin from lignin: the relationship between \u03b2-O-4 linkages and vanillin yield","volume":"116","author":"Wang","year":"2018","journal-title":"Ind. Crop. Prod."},{"issue":"8","key":"10.1016\/j.ijbiomac.2025.148985_bb0030","doi-asserted-by":"crossref","first-page":"3645","DOI":"10.1111\/1750-3841.15837","article-title":"Olfactory impact of guaiacol, ortho-vanillin, 5-methyl, and 5-formyl-vanillin as byproducts in synthetic vanillin","volume":"86","author":"Yu","year":"2021","journal-title":"J. Food Sci."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0035","article-title":"Bioproduction of high-concentration 4-vinylguaiacol using whole-cell catalysis harboring an organic solvent-tolerant phenolic acid decarboxylase from Bacillus atrophaeus [Original Research]","volume":"10\u20132019","author":"Li","year":"2019","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0040","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.jbiotec.2018.07.021","article-title":"Biosynthesis of 4-vinylguaiacol from crude ferulic acid by Bacillus licheniformis DLF-17056","volume":"281","author":"Sun","year":"2018","journal-title":"J. Biotechnol."},{"issue":"11","key":"10.1016\/j.ijbiomac.2025.148985_bb0045","first-page":"323","article-title":"Research progress in phenolic acid decarboxylase derived from microorganisms","volume":"45","author":"Yinzhu","year":"2024","journal-title":"Food Sci."},{"issue":"9","key":"10.1016\/j.ijbiomac.2025.148985_bb0050","doi-asserted-by":"crossref","first-page":"3575","DOI":"10.1021\/acssuschemeng.3c06513","article-title":"Stability increase of phenolic acid decarboxylase by a combination of protein and solvent engineering unlocks applications at elevated temperatures","volume":"12","author":"Myrtollari","year":"2024","journal-title":"ACS Sustain. Chem. Eng."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0055","doi-asserted-by":"crossref","DOI":"10.1016\/j.fbio.2023.102953","article-title":"Cloning and characterization of phenolic acid decarboxylase responsible for aromatic volatile phenols production in Paocai based on metatranscriptomics","volume":"55","author":"Zhao","year":"2023","journal-title":"Food Biosci."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0060","series-title":"Characterization of <em>Brettanomyces bruxellensis<\/em> phenolic acid decarboxylase enzyme expressed in <em>E. coli<\/em&gt. bioRxiv","author":"Lentz","year":"2024"},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.148985_bb0065","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1007\/s10295-011-0998-4","article-title":"Purification and properties of phenolic acid decarboxylase from Candida guilliermondii","volume":"39","author":"Huang","year":"2012","journal-title":"J. Ind. Microbiol. Biotechnol."},{"issue":"7","key":"10.1016\/j.ijbiomac.2025.148985_bb0070","doi-asserted-by":"crossref","first-page":"2032","DOI":"10.1038\/s41596-023-00828-5","article-title":"Encapsulating and stabilizing enzymes using hydrogen-bonded organic frameworks","volume":"18","author":"Chen","year":"2023","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0075","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2024.137856","article-title":"PVP-assisted in situ immobilizing lipase on covalent organic framework for enhanced catalytic activity and stability in bioconversions","volume":"283","author":"Zhang","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0080","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.125729","article-title":"Review of covalent organic frameworks for enzyme immobilization: strategies, applications, and prospects","volume":"248","author":"Feng","year":"2023","journal-title":"Int. J. Biol. Macromol."},{"issue":"31","key":"10.1016\/j.ijbiomac.2025.148985_bb0085","doi-asserted-by":"crossref","first-page":"40371","DOI":"10.1021\/acsami.4c06556","article-title":"Enzyme immobilization using covalent organic frameworks: from synthetic strategy to COFs functional role","volume":"16","author":"Fan","year":"2024","journal-title":"ACS Appl. Mater. Interfaces"},{"issue":"23","key":"10.1016\/j.ijbiomac.2025.148985_bb0090","doi-asserted-by":"crossref","DOI":"10.1002\/anie.202303001","article-title":"Insight into bioactivity of in-situ trapped enzyme-covalent-organic frameworks","volume":"62","author":"Liang","year":"2023","journal-title":"Angew. Chem. Int. Ed."},{"issue":"39","key":"10.1016\/j.ijbiomac.2025.148985_bb0095","doi-asserted-by":"crossref","DOI":"10.1002\/anie.202208744","article-title":"Green and scalable fabrication of high-performance biocatalysts using covalent organic frameworks as enzyme carriers","volume":"61","author":"Zheng","year":"2022","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0100","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.procbio.2018.12.034","article-title":"Secretory expression and optimization of Bacillus pumilus CotA-laccase mutant GWLF in Pichia pastoris and its mechanism on Evans blue degradation","volume":"78","author":"Xia","year":"2019","journal-title":"Process Biochem."},{"issue":"6","key":"10.1016\/j.ijbiomac.2025.148985_bb0105","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1016\/j.fm.2008.04.015","article-title":"Rational selection of non-Saccharomyces wine yeasts for mixed starters based on ester formation and enological traits","volume":"25","author":"Viana","year":"2008","journal-title":"Food Microbiol."},{"issue":"7","key":"10.1016\/j.ijbiomac.2025.148985_bb0110","doi-asserted-by":"crossref","first-page":"1870","DOI":"10.1093\/molbev\/msw054","article-title":"MEGA7: molecular evolutionary genetics analysis version 7.0 for bigger datasets","volume":"33","author":"Kumar","year":"2016","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0115","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2025.140429","article-title":"Cloning and functional characterization of the caffeine oxidase gene CsCDH from Camellia sinensis","volume":"302","author":"Zhu","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"issue":"5","key":"10.1016\/j.ijbiomac.2025.148985_bb0120","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1016\/S1872-2067(18)63033-5","article-title":"Cloning, overexpression, and characterization of a novel organic solvent-tolerant lipase from Paenibacillus pasadenensis CS0611","volume":"39","author":"Gao","year":"2018","journal-title":"Chin. J. Catal."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0125","doi-asserted-by":"crossref","DOI":"10.1016\/j.enzmictec.2024.110532","article-title":"The synthesis of cinnamyl acetate and deacetyl-7-aminocephalosporanic acid by a GDSL-type esterase and its substrate specificity analysis","volume":"182","author":"Xing","year":"2025","journal-title":"Enzyme Microb. Technol."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0130","doi-asserted-by":"crossref","DOI":"10.1016\/j.crfs.2024.100730","article-title":"Surface-displayed phenolic acid decarboxylase for increased vinylphenolic pyranoanthocyanins in blueberry wine","volume":"8","author":"Deng","year":"2024","journal-title":"Curr. Res. Food Sci."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0135","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodchem.2023.137956","article-title":"Enhancement of pyranoanthocyanin formation in blueberry wine with non-Saccharomyces yeasts","volume":"438","author":"Zhou","year":"2024","journal-title":"Food Chem."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0140","doi-asserted-by":"crossref","first-page":"3332","DOI":"10.1016\/j.ijbiomac.2020.08.205","article-title":"Molecular analysis of Bacillus velezensis KB 2216, purification and biochemical characterization of alpha-amylase","volume":"164","author":"Bhatt","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"issue":"6","key":"10.1016\/j.ijbiomac.2025.148985_bb0145","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1021\/acs.jchemed.6b00629","article-title":"Linear or nonlinear least-squares analysis of kinetic data?","volume":"94","author":"Perrin","year":"2017","journal-title":"J. Chem. Educ."},{"issue":"10","key":"10.1016\/j.ijbiomac.2025.148985_bb0150","doi-asserted-by":"crossref","first-page":"3080","DOI":"10.1038\/s41596-023-00868-x","article-title":"Enzyme immobilization on covalent organic framework supports","volume":"18","author":"Zhu","year":"2023","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0155","author":"Wang"},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0160","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.procbio.2019.11.026","article-title":"Parameters necessary to define an immobilized enzyme preparation","volume":"90","author":"Boudrant","year":"2020","journal-title":"Process Biochem."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0165","article-title":"Covalent organic framework immobilized lipase for efficient green synthesis of 1, 3-dioleoyl-2-palmitoylglycerol","volume":"552","author":"Feng","year":"2024","journal-title":"Mol. Catal."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0170","article-title":"Molecular cloning, characterization, and structural stability analysis of a rare acidic catechol 2,3-dioxygenase from the metagenome of coal-polluted soil","volume":"311","author":"Wang","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0175","doi-asserted-by":"crossref","DOI":"10.1177\/11779322241234767","article-title":"Enzymatic performance of Aspergillus oryzae \u03b1-amylase in the presence of organic solvents: activity, stability, and bioinformatic studies","volume":"18","author":"Hasan","year":"2024","journal-title":"Bioinform. Biol. Insights"},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0180","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.jbiotec.2021.12.013","article-title":"Characterization of free and immobilized lipase from Penicillium sp. onto three modified bentonites: a comparative study","volume":"344","author":"Pourkhanali","year":"2022","journal-title":"J. Biotechnol."},{"issue":"4","key":"10.1016\/j.ijbiomac.2025.148985_bb0185","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1111\/lam.12783","article-title":"Co-expression of lipase isozymes for enhanced expression in Pichia pastoris","volume":"65","author":"Cai","year":"2017","journal-title":"Lett. Appl. Microbiol."},{"issue":"11","key":"10.1016\/j.ijbiomac.2025.148985_bb0190","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1002\/elps.202200027","article-title":"A comparison between analytical approaches for molecular weight estimation of proteins with variable levels of glycosylation","volume":"43","author":"Puranik","year":"2022","journal-title":"Electrophoresis"},{"issue":"24","key":"10.1016\/j.ijbiomac.2025.148985_bb0195","doi-asserted-by":"crossref","first-page":"14877","DOI":"10.1021\/acscatal.1c03330","article-title":"Binding affinity determines substrate specificity and enables discovery of substrates for N-myristoyltransferases","volume":"11","author":"Su","year":"2021","journal-title":"ACS Catal."},{"issue":"23","key":"10.1016\/j.ijbiomac.2025.148985_bb0200","doi-asserted-by":"crossref","first-page":"7413","DOI":"10.1021\/bi036330o","article-title":"Manipulation of the Active Site Loops of d-Hydantoinase, a (\u03b2\/\u03b1)8-Barrel Protein, for Modulation of the Substrate Specificity","volume":"43","author":"Cheon","year":"2004","journal-title":"Biochemistry"},{"issue":"2","key":"10.1016\/j.ijbiomac.2025.148985_bb0205","doi-asserted-by":"crossref","DOI":"10.3390\/bioengineering11020181","article-title":"A new phenolic acid decarboxylase from the brown-rot fungus neolentinus lepideus natively decarboxylates biosourced sinapic acid into canolol, a bioactive phenolic compound","volume":"11","author":"Odinot","year":"2024","journal-title":"Bioengineering"},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0210","doi-asserted-by":"crossref","DOI":"10.1016\/j.jhazmat.2023.132261","article-title":"Enzyme-immobilized hierarchically porous covalent organic framework biocomposite for catalytic degradation of broad-range emerging pollutants in water","volume":"459","author":"Elmerhi","year":"2023","journal-title":"J. Hazard. Mater."},{"issue":"6","key":"10.1016\/j.ijbiomac.2025.148985_bb0215","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1007\/s10295-010-0709-6","article-title":"Gene cloning, expression, and characterization of phenolic acid decarboxylase from Lactobacillus brevis RM84","volume":"37","author":"Landete","year":"2010","journal-title":"J. Ind. Microbiol. Biotechnol."},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.148985_bb0220","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1271\/bbb.70496","article-title":"Identification of the 4-hydroxycinnamate decarboxylase (PAD) gene of klebsiella oxytoca","volume":"72","author":"Uchiyama","year":"2008","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0225","doi-asserted-by":"crossref","DOI":"10.1016\/j.eti.2024.103796","article-title":"In situ immobilization multi-enzyme biocatalytic system on covalent organic frameworks for efficient conversion of lignocellulose to glucose","volume":"36","author":"Tian","year":"2024","journal-title":"Environ. Technol. Innov."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0230","doi-asserted-by":"crossref","DOI":"10.1016\/j.micromeso.2019.109700","article-title":"Integration of \u03b1-amylase into covalent organic framework for highly efficient biocatalyst","volume":"291","author":"Samui","year":"2020","journal-title":"Microporous Mesoporous Mater."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0235","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1016\/j.ijbiomac.2020.12.002","article-title":"Covalent organic frameworks as emerging host platforms for enzyme immobilization and robust biocatalysis \u2013 a review","volume":"167","author":"Gan","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0240","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodres.2022.110955","article-title":"Effects of environmental factors on the microbial community changes during medium-high temperature Daqu manufacturing","volume":"153","author":"Zhu","year":"2022","journal-title":"Food Res. Int."},{"issue":"2","key":"10.1016\/j.ijbiomac.2025.148985_bb0245","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.jbiosc.2018.02.009","article-title":"Characterization and induction of phenolic acid decarboxylase from Aspergillus luchuensis","volume":"126","author":"Maeda","year":"2018","journal-title":"J. Biosci. Bioeng."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0250","first-page":"1","article-title":"Heterologous expression and enzymatic characterisation of ferulic acid decarboxylase","author":"Hexia","year":"2025","journal-title":"Food Ferment. Ind."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0255","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.renene.2021.02.065","article-title":"One-step direct transesterification of wet yeast for biodiesel production catalyzed by magnetic nanoparticle-immobilized lipase","volume":"171","author":"Cao","year":"2021","journal-title":"Renew. Energy"},{"issue":"10","key":"10.1016\/j.ijbiomac.2025.148985_bb0260","doi-asserted-by":"crossref","first-page":"1739","DOI":"10.1007\/s00449-022-02783-z","article-title":"Degradation of 2,4-DCP by the immobilized laccase on the carrier of sodium alginate-sodium carboxymethyl cellulose","volume":"45","author":"Zhao","year":"2022","journal-title":"Bioprocess Biosyst. Eng."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0265","first-page":"25","article-title":"Cloning, expression and immobilisation of recombinant phenolic acid decarboxylase from Escherichia coli","volume":"11","author":"Ting","year":"2021","journal-title":"Brew. Technol."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0270","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.bios.2014.07.057","article-title":"Surface modification of silicon dioxide, silicon nitride and titanium oxynitride for lactate dehydrogenase immobilization","volume":"67","author":"Saengdee","year":"2015","journal-title":"Biosens. Bioelectron."},{"key":"10.1016\/j.ijbiomac.2025.148985_bb0275","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.biortech.2018.04.114","article-title":"Saccharification of Spirulina platensis biomass using free and immobilized amylolytic enzymes","volume":"263","author":"Rempel","year":"2018","journal-title":"Bioresour. Technol."}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S014181302509542X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S014181302509542X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T04:24:01Z","timestamp":1781843041000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S014181302509542X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,1]]},"references-count":55,"alternative-id":["S014181302509542X"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.148985","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2026,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"A novel heat-resistant hydroxycinnamic acid decarboxylase from Wickerhamomyces anomalus","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.148985","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier B.V. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"148985"}}