{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T13:52:22Z","timestamp":1791294742136,"version":"4.1.0"},"reference-count":58,"publisher":"American Chemical Society (ACS)","issue":"19","license":[{"start":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T00:00:00Z","timestamp":1788998400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T00:00:00Z","timestamp":1788998400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T00:00:00Z","timestamp":1788998400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100004854","name":"New York State Department of Agriculture and Markets","doi-asserted-by":"publisher","award":["2024-67011-42996"],"award-info":[{"award-number":["2024-67011-42996"]}],"id":[{"id":"10.13039\/100004854","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100005825","name":"National Institute of Food and Agriculture","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100005825","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007513","name":"Dairy Management","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007513","id-type":"DOI","asserted-by":"publisher"}]},{"name":"New York State Milk Promotion Advisory Board"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,6]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The development of stable and recyclable biocatalysts is vital for sustainable bioprocessing. In this study, we demonstrated fusion of l-arabinose isomerase from Thermotoga neapolitana (TnAI) with a cellulose-binding module (CBM) to facilitate direct, noncovalent immobilization on cellulose fibers for the biocatalytic transformation of d-galactose to d-tagatose. The impact of His-tag positioning on TnAI activity and quaternary structure was initially assessed, revealing that the C-terminal tag caused enzyme aggregation and loss of activity. In contrast, the N-terminal His-tag preserved the hexameric configuration and catalytic efficiency. Three CBM-TnAI fusion variants containing flexible linkers (L1\u2013L3) were subsequently generated, expressed, and purified. All CBM-fused variants retained solubility and catalytic activity comparable to the native enzyme, confirming that the N-terminal CBM fusion does not disrupt active-site conformation. Immobilization studies on microcrystalline cellulose showed high binding efficiencies (&amp;gt;80%) and substantial retention of catalytic activity, with CBM_L2_TnAI exhibiting the highest cellulose-binding efficiency (&amp;gt;90%) and immobilized activity (\u223c87%). Consistent with its superior catalytic performance and immobilization characteristics, CBM_L2_TnAI was selected for reusability studies and retained approximately 40% of its initial activity after five reaction cycles, demonstrating good operational stability. This CBM-mediated immobilization strategy eliminates the need for chemical cross-linkers, providing a simple, cost-effective, and sustainable platform for producing reusable enzyme systems. The cellulose-protein hybrid catalyst developed herein offers a versatile framework for continuous or batch biotransformation of low-value waste carbohydrates into value-added rare sugars.<\/jats:p>","DOI":"10.1021\/acs.biochem.6c00239","type":"journal-article","created":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T16:01:26Z","timestamp":1789056086000},"page":"3057-3065","source":"Crossref","is-referenced-by-count":0,"title":["Cellulose-Binding\nModule-Mediated Immobilization of\n                    <scp>l<\/scp>\n                    -Arabinose Isomerase\nfor Reusable\n                    <scp>d<\/scp>\n                    -Tagatose\nProduction"],"prefix":"10.1021","volume":"65","author":[{"given":"Amol D.","family":"Pagar","sequence":"first","affiliation":[{"name":"Cornell University , , , ,","place":["Ithaca, New York, United States, 14850"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9021-8809","authenticated-orcid":true,"given":"Sonia","family":"Su","sequence":"additional","affiliation":[{"name":"Cornell University , , , ,","place":["Ithaca, New York, United States, 14850"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhixin","family":"Wang","sequence":"additional","affiliation":[{"name":"Cornell University , , , ,","place":["Ithaca, New York, United States, 14850"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3644-0732","authenticated-orcid":true,"given":"Julie M.","family":"Goddard","sequence":"additional","affiliation":[{"name":"Cornell University , , , ,","place":["Ithaca, New York, United States, 14850"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,10]]},"reference":[{"key":"2026100608064079300_cit1","doi-asserted-by":"publisher","first-page":"18511","DOI":"10.1021\/acs.jafc.5c04610","article-title":"Recent advances on\nbiological production of a functional low-calorie sugar D-tagatose","volume":"73","author":"Fan","year":"2025","journal-title":"J. Agric. Food Chem."},{"key":"2026100608064079300_cit2","doi-asserted-by":"publisher","first-page":"46","DOI":"10.3390\/fermentation11020046","article-title":"Advances in\nbiological production of D-tagatose: a comprehensive overview","volume":"11","author":"Zhang","year":"2025","journal-title":"Fermentation"},{"key":"2026100608064079300_cit3","doi-asserted-by":"publisher","first-page":"1492","DOI":"10.1080\/07388551.2025.2489424","article-title":"Biosynthesis\nof a healthy natural sugar D-tagatose:\nadvances and opportunities","volume":"45","author":"Fan","year":"2025","journal-title":"Crit. Rev. Biotechnol."},{"key":"2026100608064079300_cit4","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s00253-007-0981-1","article-title":"Tagatose:\nproperties, applications, and biotechnological processes","volume":"76","author":"Oh","year":"2007","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"2026100608064079300_cit5","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1155\/2018\/8718053","article-title":"D-Tagatose\nis a promising sweetener to control glycaemia: a new functional food","volume":"2018","author":"Guerrero-Wyss","year":"2018","journal-title":"BioMed Res. Int."},{"key":"2026100608064079300_cit6","doi-asserted-by":"publisher","first-page":"767944","DOI":"10.3389\/fcimb.2021.767944","article-title":"Potential\nof prebiotic D-tagatose\nfor prevention of oral disease","volume":"11","author":"Mayumi","year":"2021","journal-title":"Front. Cell.\nInfect. Microbiol."},{"key":"2026100608064079300_cit7","doi-asserted-by":"publisher","first-page":"5679","DOI":"10.1080\/10408398.2021.1895057","article-title":"A head-to-head comparison\nreview of biological and toxicological\nstudies of isomaltulose, D-tagatose, and trehalose on glycemic control","volume":"62","author":"Soko\u0142owska","year":"2022","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"2026100608064079300_cit8","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1089\/109662002753723197","article-title":"Tagatose,\nthe new GRAS sweetener and health product","volume":"5","author":"Levin","year":"2002","journal-title":"J.\nMed. Food"},{"key":"2026100608064079300_cit9","doi-asserted-by":"publisher","first-page":"24","DOI":"10.1016\/j.catcom.2018.01.011","article-title":"Catalytic\nisomerization of galactose into tagatose\nin the presence of bases and Lewis acids","volume":"107","author":"Drabo","year":"2018","journal-title":"Catal.\nCommun."},{"key":"2026100608064079300_cit10","doi-asserted-by":"publisher","first-page":"3430","DOI":"10.1080\/10408398.2015.1126550","article-title":"Biocatalytic\nproduction of D-tagatose: a potential rare sugar with versatile applications","volume":"57","author":"Jayamuthunagai","year":"2017","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"2026100608064079300_cit11","doi-asserted-by":"publisher","first-page":"569","DOI":"10.1016\/j.tifs.2020.11.020","article-title":"Harnessing\nL-arabinose isomerase for biological production of D-tagatose: recent\nadvances and its applications","volume":"108","author":"Ravikumar","year":"2021","journal-title":"Trends Food Sci.\nTechnol."},{"key":"2026100608064079300_cit12","doi-asserted-by":"publisher","first-page":"385","DOI":"10.1007\/s12033-019-00161-x","article-title":"Biochemical characterization of heat-tolerant\nrecombinant L-arabinose isomerase from Enterococcus faecium DBFIQ E36 strain with feasible applications in D-tagatose production","volume":"61","author":"Manzo","year":"2019","journal-title":"Mol. Biotechnol."},{"key":"2026100608064079300_cit13","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1186\/s12896-016-0286-5","article-title":"Characterization\nof an L-arabinose isomerase from Bacillus coagulans NL01 and its application for D-tagatose production","volume":"16","author":"Mei","year":"2016","journal-title":"BMC Biotechnol."},{"key":"2026100608064079300_cit14","doi-asserted-by":"publisher","first-page":"441","DOI":"10.1007\/s00792-011-0375-2","article-title":"Identification and characterization\nof a novel L-arabinose isomerase from Anoxybacillus flavithermus useful in D-tagatose production","volume":"15","author":"Li","year":"2011","journal-title":"Extremophiles"},{"key":"2026100608064079300_cit15","doi-asserted-by":"publisher","first-page":"162","DOI":"10.1016\/j.jbiotec.2005.06.004","article-title":"Purification and\ncharacterization of an L-arabinose isomerase from\nan isolated strain of Geobacillus thermodenitrificans producing D-tagatose","volume":"120","author":"Kim","year":"2005","journal-title":"J. Biotechnol."},{"key":"2026100608064079300_cit16","doi-asserted-by":"publisher","first-page":"4696","DOI":"10.3390\/app12094696","article-title":"Characterization\nof L-arabinose isomerase from Klebsiella pneumoniae and its application in the production of D-tagatose from D-galactose","volume":"12","author":"Shin","year":"2022","journal-title":"Appl. Sci."},{"key":"2026100608064079300_cit17","doi-asserted-by":"publisher","first-page":"1839","DOI":"10.1007\/s00253-009-2210-6","article-title":"Characterization\nof an L-arabinose\nisomerase from Bacillus subtilis","volume":"85","author":"Kim","year":"2010","journal-title":"Appl. Microbiol. 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Adv."},{"key":"2026100608064079300_cit27","doi-asserted-by":"publisher","first-page":"1222","DOI":"10.3390\/catal11101222","article-title":"Current\nstatus and future perspectives of supports\nand protocols for enzyme immobilization","volume":"11","author":"Cavalcante","year":"2021","journal-title":"Catalysts"},{"key":"2026100608064079300_cit28","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1016\/j.cofs.2021.09.004","article-title":"Food enzymes immobilization: novel\ncarriers, techniques and applications","volume":"43","author":"Xie","year":"2022","journal-title":"Curr.\nOpin. Food Sci."},{"key":"2026100608064079300_cit29","doi-asserted-by":"publisher","DOI":"10.1111\/1750-3841.70606","article-title":"Optimized\ncross-linked enzyme aggregates\nfor lactose conversion in whey","volume":"90","author":"Dellamea","year":"2025","journal-title":"J. Food Sci."},{"key":"2026100608064079300_cit30","doi-asserted-by":"publisher","first-page":"140390","DOI":"10.1016\/j.ijbiomac.2025.140390","article-title":"Trehalose decorated nanostructures\nstabilize combined\ncross-linked enzyme aggregates (Combi-CLEAs) of \u03b2-galactosidase\nand glucose isomerase","volume":"302","author":"Scott","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"key":"2026100608064079300_cit31","doi-asserted-by":"publisher","first-page":"1684","DOI":"10.1080\/10643389.2023.2180285","article-title":"Enzyme immobilization\nas a sustainable\napproach toward ecological remediation of organic-contaminated soils:\nadvances, issues, and future perspectives","volume":"53","author":"Wang","year":"2023","journal-title":"Crit.\nRev. Environ. Sci. Technol."},{"key":"2026100608064079300_cit32","doi-asserted-by":"publisher","first-page":"358","DOI":"10.1016\/j.biotechadv.2015.02.006","article-title":"Recombinant CBM-fusion\ntechnology: applications overview","volume":"33","author":"Oliveira","year":"2015","journal-title":"Biotechnol.\nAdv."},{"key":"2026100608064079300_cit33","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.cbpa.2019.11.008","article-title":"Protein immobilization\ntechnology for flow biocatalysis","volume":"55","author":"Romero-Ferna\u0301ndez","year":"2020","journal-title":"Curr. Opin.\nChem. Biol."},{"key":"2026100608064079300_cit34","doi-asserted-by":"publisher","first-page":"708","DOI":"10.1007\/s12010-012-9811-8","article-title":"Efficiency\nand stability enhancement of cis-epoxysuccinic acid hydrolase by fusion\nwith a carbohydrate-binding module and immobilization onto cellulose","volume":"168","author":"Wang","year":"2012","journal-title":"Appl. Biochem. Biotechnol."},{"key":"2026100608064079300_cit35","doi-asserted-by":"publisher","first-page":"110782","DOI":"10.1016\/j.enzmictec.2025.110782","article-title":"Silica immobilized PETase for microplastic\nbioremediation: influence of linker peptides on activity","volume":"193","author":"Su","year":"2026","journal-title":"Enzyme Microb. Technol."},{"key":"2026100608064079300_cit36","doi-asserted-by":"publisher","first-page":"283","DOI":"10.1128\/MMBR.00028-05","article-title":"Carbohydrate-binding\nmodules: biochemical\nproperties and novel applications","volume":"70","author":"Shoseyov","year":"2006","journal-title":"Microbiol.\nMol. Biol. Rev."},{"key":"2026100608064079300_cit37","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1016\/S0734-9750(02)00006-X","article-title":"Cellulose-binding domains:\nbiotechnological applications","volume":"20","author":"Levy","year":"2002","journal-title":"Biotechnol. 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Lett."},{"key":"2026100608064079300_cit42","doi-asserted-by":"publisher","first-page":"476","DOI":"10.1016\/j.ijbiomac.2018.04.081","article-title":"Development of enzymatically\nactive bacterial cellulose membranes through stable immobilization\nof an engineered \u03b2-galactosidase","volume":"115","author":"Estevinho","year":"2018","journal-title":"Int.\nJ. Biol. Macromol."},{"key":"2026100608064079300_cit43","doi-asserted-by":"publisher","first-page":"207","DOI":"10.1016\/j.fbp.2021.01.010","article-title":"Recombinant lactase\nwith a cellulose-binding domain permits facile immobilization onto\ncellulose with retained activity","volume":"126","author":"Wang","year":"2021","journal-title":"Food Bioprod.\nProcess."},{"key":"2026100608064079300_cit44","doi-asserted-by":"publisher","first-page":"711","DOI":"10.1093\/protein\/14.9.711","article-title":"Stable linker\npeptides for a cellulose-binding domain\u2013lipase\nfusion protein expressed in Pichia pastoris","volume":"14","author":"Gustavsson","year":"2001","journal-title":"Protein Eng."},{"key":"2026100608064079300_cit45","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1016\/j.bbrc.2012.02.139","article-title":"Increased\nthermal stability and cellulose-binding\ncapacity of Cryptococcus sp. 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Bioeng."},{"key":"2026100608064079300_cit48","doi-asserted-by":"publisher","first-page":"5739","DOI":"10.1002\/j.1460-2075.1996.tb00960.x","article-title":"Crystal\nstructure of a bacterial\nfamily-III cellulose-binding domain: a general mechanism for attachment\nto cellulose","volume":"15","author":"Tormo","year":"1996","journal-title":"EMBO J."},{"key":"2026100608064079300_cit49","doi-asserted-by":"publisher","first-page":"1357","DOI":"10.1016\/j.addr.2012.09.039","article-title":"Fusion\nprotein linkers: property,\ndesign and functionality","volume":"65","author":"Chen","year":"2013","journal-title":"Adv. Drug Deliv Rev."},{"key":"2026100608064079300_cit50","doi-asserted-by":"publisher","first-page":"208","DOI":"10.1021\/bp000147u","article-title":"High production\nof D-tagatose, a potential sugar substitute, using immobilized L-arabinose\nisomerase","volume":"17","author":"Kim","year":"2001","journal-title":"Biotechnol. Prog."},{"key":"2026100608064079300_cit51","doi-asserted-by":"publisher","first-page":"400","DOI":"10.1021\/bp025675f","article-title":"A feasible enzymatic\nprocess for D-tagatose production by an immobilized thermostable L-arabinose\nisomerase in a packed-bed bioreactor","volume":"19","author":"Kim","year":"2003","journal-title":"Biotechnol.\nProg."},{"key":"2026100608064079300_cit52","doi-asserted-by":"publisher","first-page":"102227","DOI":"10.1016\/j.bcab.2021.102227","article-title":"Production of D-tagatose\nin packed bed reactor containing\nan immobilized L-arabinose isomerase on alginate support","volume":"38","author":"Rai","year":"2021","journal-title":"Biocatal. Agric. Biotechnol."},{"key":"2026100608064079300_cit53","doi-asserted-by":"publisher","first-page":"1538","DOI":"10.3390\/foods14091538","article-title":"Enabling stable recycling of L-arabinose\nisomerase through whole-cell immobilization for efficient and cost-effective\nD-tagatose production","volume":"14","author":"Li","year":"2025","journal-title":"Foods"},{"key":"2026100608064079300_cit54","doi-asserted-by":"publisher","first-page":"109566","DOI":"10.1016\/j.enzmictec.2020.109566","article-title":"Preparation\nof CLEAs and magnetic CLEAs of a recombinant L-arabinose isomerase\nfor D-tagatose synthesis","volume":"138","author":"de Sousa","year":"2020","journal-title":"Enzyme Microb. 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