{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,11]],"date-time":"2026-05-11T05:08:57Z","timestamp":1778476137159,"version":"3.51.4"},"reference-count":87,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,5,11]],"date-time":"2026-05-11T00:00:00Z","timestamp":1778457600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Microbiol."],"abstract":"<jats:p>\n                    Chitin, the second most abundant polysaccharide, is poorly soluble and underutilized, whereas its monomer N-acetylglucosamine (GlcNAc) has broad pharmaceutical applications. Efficient enzymatic conversion of chitin to GlcNAc remains challenging.\n                    <jats:italic>Chitinibacter mangrovi<\/jats:italic>\n                    FCG-7\n                    <jats:sup>T<\/jats:sup>\n                    , a novel chitinolytic strain isolated from mangrove sediments, exhibited exceptional chitin degradation, achieving a hydrolysis zone ratio (H\/C) of 4.75 and maintained genetic stability over ten successive passages. Sequential optimization using One-Factor-at-a-Time (OFAT), Plackett-Burman designs (PBD), and Box\u2013Behnken designs (BBD) enhanced chitinase production by 49.43-fold, yielding a final activity of 1.211\u202fU\/mL under optimized conditions (pH 7.4, 20\u202f\u00b0C, 12\u202fg\/L powdered chitin). Purification yielded a 100\u202fkDa bifunctional chitinase\n                    <jats:italic>Cm<\/jats:italic>\n                    Chi, exhibiting dual chitobiosidase and N-acetylglucosaminidase (NAGase) activities. The purified enzyme showed a specific activity of 7.96\u202fU\/mg toward colloidal chitin.\n                    <jats:italic>Cm<\/jats:italic>\n                    Chi demonstrated a high affinity for colloidal chitin with a\n                    <jats:italic>\n                      K\n                      <jats:sub>m<\/jats:sub>\n                    <\/jats:italic>\n                    value of 0.24\u202fmg\/mL and retained over 80% stability across a broad pH range 4.0\u201311.0. Furthermore,\n                    <jats:italic>Cm<\/jats:italic>\n                    Chi completely converted colloidal chitin to N-acetylglucosamine (GlcNAc) within 48\u202fh and demonstrated tolerance to various reagents, including 1% methanol, acetonitrile, Tween 20, and Tween 80 (v\/v). Notably, in cyclophosphamide (CTX)-induced immunosuppressed mice, GlcNAc (200\u202fmg\/kg) significantly restored body weight, thymic\/splenic indices, and tissue architecture while elevating serum TNF-\n                    <jats:italic>\u03b1<\/jats:italic>\n                    , IL-2, IgG, and IgM (\n                    <jats:italic>p<\/jats:italic>\n                    \u202f&amp;lt;\u202f0.05). This study establishes\n                    <jats:italic>Cm<\/jats:italic>\n                    Chi as an efficient biocatalyst for industrial GlcNAc production and validates the immunomodulatory potential of GlcNAc, highlighting its dual applicability in biotechnology and immunotherapy.\n                  <\/jats:p>","DOI":"10.3389\/fmicb.2026.1826206","type":"journal-article","created":{"date-parts":[[2026,5,11]],"date-time":"2026-05-11T04:25:35Z","timestamp":1778473535000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["Highly efficient chitinase production from Chitinibacter mangrovi FCG-7T and immunomodulatory efficacy of generated GlcNAc in cyclophosphamide-induced immunosuppression"],"prefix":"10.3389","volume":"17","author":[{"given":"Longzhi","family":"Chen","sequence":"first","affiliation":[{"name":"College of Life Science and Technology, Guangxi University","place":["Nanning, Guangxi, China"]},{"name":"State Key Laboratory of Non-food Biomass Energy Technology, Guangxi Key Laboratory of Marine Natural Products and Combinatorial Biosynthesis Chemistry, Guangxi Academy of Marine Sciences, Guangxi Academy of Sciences","place":["Nanning, Guangxi, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jianong","family":"Wang","sequence":"additional","affiliation":[{"name":"Guangxi Testing Center for Medical Devices","place":["Nanning, Guangxi, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zixuan","family":"Zhang","sequence":"additional","affiliation":[{"name":"College of Life Science and Technology, Guangxi University","place":["Nanning, Guangxi, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lixia","family":"Pan","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Non-food Biomass Energy Technology, Guangxi Key Laboratory of Marine Natural Products and Combinatorial Biosynthesis Chemistry, Guangxi Academy of Marine Sciences, Guangxi Academy of Sciences","place":["Nanning, Guangxi, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dengfeng","family":"Yang","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Non-food Biomass Energy Technology, Guangxi Key Laboratory of Marine Natural Products and Combinatorial Biosynthesis Chemistry, Guangxi Academy of Marine Sciences, Guangxi Academy of Sciences","place":["Nanning, Guangxi, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nan","family":"Li","sequence":"additional","affiliation":[{"name":"College of Life Science and Technology, Guangxi University","place":["Nanning, Guangxi, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Liyan","family":"Yang","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Non-food Biomass Energy Technology, Guangxi Key Laboratory of Marine Natural Products and Combinatorial Biosynthesis Chemistry, Guangxi Academy of Marine Sciences, Guangxi Academy of Sciences","place":["Nanning, Guangxi, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1965","published-online":{"date-parts":[[2026,5,11]]},"reference":[{"key":"ref1","doi-asserted-by":"publisher","first-page":"797","DOI":"10.1080\/10826068.2022.2140356","article-title":"Purification and characterization of Stenotrophomonas maltophilia chitinase with antifungal and insecticidal properties","volume":"53","author":"Aktas","year":"2023","journal-title":"Prep. 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Microbiol."},{"key":"ref5","doi-asserted-by":"publisher","first-page":"338","DOI":"10.1016\/j.ijbiomac.2017.08.026","article-title":"Biochemical characterization of a novel thermostable chitinase from Hydrogenophilus hirschii strain KB-DZ44","volume":"106","author":"Bouacem","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref6","doi-asserted-by":"publisher","first-page":"6863","DOI":"10.1039\/D1FO01118C","article-title":"Alhagi honey polysaccharides attenuate intestinal injury and immune suppression in cyclophosphamide-induced mice","volume":"12","author":"Cai","year":"2021","journal-title":"Food Funct."},{"key":"ref7","doi-asserted-by":"publisher","first-page":"114","DOI":"10.1007\/s11274-019-2694-x","article-title":"Bioproduction of N-acetyl-glucosamine from colloidal \u03b1-chitin using an enzyme cocktail produced by Aeromonas caviae CHZ306","volume":"35","author":"Cardozo","year":"2019","journal-title":"World J. Microbiol. 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Macromol."},{"key":"ref12","doi-asserted-by":"publisher","first-page":"524","DOI":"10.1016\/j.fsi.2014.08.008","article-title":"N-acetylglucosamine enhances survival ability of tilapias infected by Streptococcus iniae","volume":"40","author":"Cheng","year":"2014","journal-title":"Fish Shellfish Immunol."},{"key":"ref14","doi-asserted-by":"publisher","first-page":"113","DOI":"10.1016\/j.ijbiomac.2019.05.035","article-title":"Heterologous expression and characterization of an antifungal chitinase (Chit46) from Trichoderma harzianum GIM 3.442 and its application in colloidal chitin conversion","volume":"134","author":"Deng","year":"2019","journal-title":"Int. J. Biol. 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Macromol."},{"key":"ref16","doi-asserted-by":"publisher","first-page":"761","DOI":"10.1007\/s10341-023-00870-3","article-title":"Antifungal activity of partially purified bacterial chitinase against Alternaria alternata","volume":"65","author":"Dikba\u015f","year":"2023","journal-title":"Erwerbs-obstbau"},{"key":"ref17","doi-asserted-by":"publisher","first-page":"3671","DOI":"10.1039\/C9FO00356D","article-title":"Modulating effects of polysaccharides from the fruits of Lycium barbarum on the immune response and gut microbiota in cyclophosphamide-treated mice","volume":"10","author":"Ding","year":"2019","journal-title":"Food Funct."},{"key":"ref18","doi-asserted-by":"publisher","first-page":"7885","DOI":"10.1021\/acs.jcim.4c01303","article-title":"qProtein: exploring physical features of protein thermostability based on structural proteomics","volume":"64","author":"Dou","year":"2024","journal-title":"J. Chem. Inf. Model."},{"key":"ref19","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1002\/bab.1889","article-title":"Purification and characterization of chitinase from Paenibacillus sp","volume":"68","author":"Du","year":"2021","journal-title":"Biotechnol. Appl. Biochem."},{"key":"ref20","doi-asserted-by":"publisher","first-page":"638","DOI":"10.1038\/nrclinonc.2009.146","article-title":"Cyclophosphamide and cancer: golden anniversary","volume":"6","author":"Emadi","year":"2009","journal-title":"Nat. Rev. Clin. Oncol."},{"key":"ref21","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1017\/S0029665114001463","article-title":"Links between diet, gut microbiota composition and gut metabolism","volume":"74","author":"Flint","year":"2015","journal-title":"Proc. Nutr. 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Biofuels"},{"key":"ref25","doi-asserted-by":"publisher","first-page":"1242","DOI":"10.1590\/S1517-83822012000400002","article-title":"Microbial diversity in Brazilian mangrove sediments: a mini review","volume":"43","author":"Ghizelini","year":"2012","journal-title":"Braz. J. Microbiol."},{"key":"ref26","doi-asserted-by":"publisher","first-page":"93","DOI":"10.3390\/md23030093","article-title":"The impact of chitinase binding domain truncation on the properties of CaChi18B from Chitinilyticum aquatile CSC-1","volume":"23","author":"Gu","year":"2025","journal-title":"Mar. Drugs"},{"key":"ref27","doi-asserted-by":"publisher","first-page":"665","DOI":"10.1016\/s1872-2067(17)62787-6","article-title":"Purification and characterization of alkaline chitinase from Paenibacillus pasadenensis CS0611","volume":"38","author":"Guo","year":"2017","journal-title":"Chin. J. 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Sci."},{"key":"ref32","doi-asserted-by":"publisher","first-page":"92","DOI":"10.1007\/s00203-025-04529-5","article-title":"A novel antifungal chitinase from Chaetomium globosum: column-free purification and characterization","volume":"207","author":"Jiang","year":"2025","journal-title":"Arch. Microbiol."},{"key":"ref33","doi-asserted-by":"publisher","first-page":"3137","DOI":"10.3892\/etm.2017.4849","article-title":"Evaluation of the chondroprotective action of N-acetylglucosamine in a rat experimental osteoarthritis model","volume":"14","author":"Kubomura","year":"2017","journal-title":"Exp. Ther. Med."},{"key":"ref34","doi-asserted-by":"publisher","first-page":"131362","DOI":"10.1016\/j.ijbiomac.2024.131362","article-title":"Response surface optimization, purification, characterization and short-chain chitooligosaccharides production from an acidic, thermostable chitinase from Thermomyces dupontii","volume":"267","author":"Kumari","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"key":"ref35","doi-asserted-by":"publisher","first-page":"470","DOI":"10.1080\/13102818.2015.1012937","article-title":"Statistical optimization of medium components for chitinase production by Pseudomonas fluorescens strain HN1205: role of chitinase on egg hatching inhibition of root-knot nematode","volume":"29","author":"Lee","year":"2015","journal-title":"Biotechnol. Biotechnol. Equip."},{"key":"ref36","doi-asserted-by":"publisher","first-page":"303","DOI":"10.1186\/s13068-018-1301-y","article-title":"Cloning, purification, and characterization of an organic solvent-tolerant chitinase, MtCh509, from Microbulbifer thermotolerans DAU221","volume":"11","author":"Lee","year":"2018","journal-title":"Biotechnol. Biofuels"},{"key":"ref37","doi-asserted-by":"publisher","first-page":"445","DOI":"10.1016\/j.carbpol.2018.05.050","article-title":"Se-enriched G. frondosa polysaccharide protects against immunosuppression in cyclophosphamide-induced mice via MAPKs signal transduction pathway","volume":"196","author":"Li","year":"2018","journal-title":"Carbohydr. Polym."},{"key":"ref38","doi-asserted-by":"publisher","first-page":"148690","DOI":"10.1016\/j.ijbiomac.2025.148690","article-title":"Clustering intramolecular interactions of proteins significantly enhances cellular thermal stability","volume":"332","author":"Li","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"key":"ref39","doi-asserted-by":"publisher","first-page":"3132","DOI":"10.1128\/JB.00148-10","article-title":"Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by \u03b2-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase","volume":"192","author":"Litzinger","year":"2010","journal-title":"J. Bacteriol."},{"key":"ref40","doi-asserted-by":"publisher","first-page":"695","DOI":"10.3390\/md17120695","article-title":"A cold-adapted chitinase-producing bacterium from Antarctica and its potential in biocontrol of plant pathogenic fungi","volume":"17","author":"Liu","year":"2019","journal-title":"Mar. Drugs"},{"key":"ref41","doi-asserted-by":"publisher","first-page":"e8964","DOI":"10.7717\/peerj.8964","article-title":"Cloning, expression and characterization of a chitinase from Paenibacillus chitinolyticus strain UMBR 0002","volume":"8","author":"Liu","year":"2020","journal-title":"PeerJ"},{"key":"ref42","doi-asserted-by":"publisher","first-page":"139675","DOI":"10.1016\/j.foodchem.2024.139675","article-title":"Enzymatic production of diverse N-acetyl chitooligosaccharides employing a novel bifunctional chitinase and its engineered variants","volume":"453","author":"Liu","year":"2024","journal-title":"Food Chem."},{"key":"ref43","doi-asserted-by":"publisher","first-page":"2892","DOI":"10.3390\/ijms21082892","article-title":"The crystal structure of a Streptomyces thermoviolaceus thermophilic chitinase known for its refolding efficiency","volume":"21","author":"Malecki","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"ref44","doi-asserted-by":"publisher","first-page":"878","DOI":"10.1007\/s12272-016-0746-4","article-title":"Purification and characterization of chitinase showing antifungal and biodegradation properties obtained from Streptomyces anulatus CS242","volume":"39","author":"Mander","year":"2016","journal-title":"Arch. Pharm. Res."},{"key":"ref45","doi-asserted-by":"publisher","first-page":"1045","DOI":"10.1038\/s41467-023-36610-0","article-title":"Enzyme adaptation to habitat thermal legacy shapes the thermal plasticity of marine microbiomes","volume":"14","author":"Marasco","year":"2023","journal-title":"Nat. Commun."},{"key":"ref46","doi-asserted-by":"publisher","first-page":"11121","DOI":"10.1021\/acs.jafc.4c10364","article-title":"Boosting biocatalytic efficiency: engineering of chitinase chit33 with chitin and cellulose binding domains for sustainable chitin conversion","volume":"73","author":"Mart\u00ednez-Ranz","year":"2025","journal-title":"J. Agric. Food Chem."},{"key":"ref47","doi-asserted-by":"publisher","first-page":"140465","DOI":"10.1016\/j.ijbiomac.2024.140465","article-title":"Exposed tryptophan residues in the chitin-binding domain of ChiA74 chitinase are important for chitin-binding and antifungal activity","volume":"302","author":"Mart\u00ednez-Zavala","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"key":"ref48","doi-asserted-by":"publisher","first-page":"15613","DOI":"10.1021\/acs.jafc.4c03077","article-title":"Three-step enzymatic remodeling of chitin into bioactive chitooligomers","volume":"72","author":"M\u00e9sz\u00e1ros","year":"2024","journal-title":"J. Agric. Food Chem."},{"key":"ref49","doi-asserted-by":"publisher","first-page":"426","DOI":"10.1021\/ac60147a030","article-title":"Use of dinitrosalicylic acid reagent for determination of reducing sugar","volume":"31","author":"Miller","year":"1959","journal-title":"Anal. Chem."},{"key":"ref50","doi-asserted-by":"publisher","first-page":"146538","DOI":"10.1016\/j.ijbiomac.2024.146538","article-title":"Structural-mechanistic insights and performance engineering of chitinase MpChit35 for tailored chito-oligosaccharide production","volume":"322","author":"Minguet-Lobato","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"key":"ref51","doi-asserted-by":"publisher","first-page":"565","DOI":"10.1007\/s10068-017-0248-2","article-title":"Immuno-enhancement effect of polysaccharide extracted from Stichopus japonicus on cyclophosphamide-induced immunosuppression mice","volume":"27","author":"Monmai","year":"2017","journal-title":"Food Sci. Biotechnol."},{"key":"ref52","doi-asserted-by":"publisher","first-page":"1543","DOI":"10.1093\/bbb\/zbad134","article-title":"A novel endo-type chitinase possessing chitobiase activity derived from the chitinolytic bacterium, Chitiniphilus shinanonensis SAY3T","volume":"87","author":"Okazaki","year":"2023","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref53","doi-asserted-by":"publisher","first-page":"933","DOI":"10.3390\/genes14040933","article-title":"The hexosamine biosynthesis pathway: regulation and function","volume":"14","author":"Paneque","year":"2023","journal-title":"Genes (Basel)"},{"key":"ref54","doi-asserted-by":"publisher","first-page":"688","DOI":"10.3390\/molecules27030688","article-title":"Polyextremophilic chitinolytic activity by a marine strain (IG119) of Clonostachys rosea","volume":"27","author":"Pasqualetti","year":"2022","journal-title":"Molecules"},{"key":"ref55","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1016\/j.cbi.2011.12.006","article-title":"Amelioration of cyclophosphamide induced myelosuppression and oxidative stress by cinnamic acid","volume":"195","author":"Patra","year":"2012","journal-title":"Chem. Biol. Interact."},{"key":"ref56","doi-asserted-by":"publisher","first-page":"100773","DOI":"10.1016\/j.carpta.2025.100773","article-title":"CAZyme analysis and functional characterization of a new GH18 chitin hydrolase from Gelidibacter salicanalis PAMC21136","volume":"10","author":"Paudel","year":"2025","journal-title":"Carbohydr. Polym. Technol. Appl."},{"key":"ref57","doi-asserted-by":"publisher","first-page":"80599","DOI":"10.18632\/oncotarget.12413","article-title":"Targeting the hexosamine biosynthetic pathway and O-linked N-acetylglucosamine cycling for therapeutic and imaging capabilities in diffuse large B-cell lymphoma","volume":"7","author":"Pham","year":"2016","journal-title":"Oncotarget"},{"key":"ref58","doi-asserted-by":"publisher","first-page":"596617","DOI":"10.3389\/fendo.2021.596617","article-title":"The role of O-GlcNAcylation in immune cell activation","volume":"12","author":"Qiang","year":"2021","journal-title":"Front. Endocrinol. (Lausanne)"},{"key":"ref59","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1016\/j.bcab.2016.01.008","article-title":"Optimised production of chitinase from a novel mangrove isolate, Bacillus pumilus MCB-7 using response surface methodology","volume":"5","author":"Rishad","year":"2016","journal-title":"Biocatal. Agric. Biotechnol."},{"key":"ref60","doi-asserted-by":"publisher","first-page":"36","DOI":"10.1016\/j.pestbp.2016.09.005","article-title":"Biocontrol potential of halotolerant bacterial chitinase from high yielding novel Bacillus pumilus MCB-7 autochthonous to mangrove ecosystem","volume":"137","author":"Rishad","year":"2017","journal-title":"Pestic. Biochem. Physiol."},{"key":"ref61","doi-asserted-by":"publisher","first-page":"3397","DOI":"10.1128\/AEM.64.9.3397-3402.1998","article-title":"Purification and characterization of three thermostable endochitinases of a noble Bacillus strain, MH-1, isolated from chitin-containing compost","volume":"64","author":"Sakai","year":"1998","journal-title":"Appl. Environ. Microbiol."},{"key":"ref62","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s11274-020-02840-3","article-title":"Biocontrol potential of chitinases produced by newly isolated Chitinophaga sp. S167","volume":"36","author":"Sharma","year":"2020","journal-title":"World J. Microbiol. 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Microbiol."},{"key":"ref67","doi-asserted-by":"publisher","first-page":"937","DOI":"10.1039\/C7FO01302G","article-title":"Effects of polysaccharides from purple sweet potatoes on immune response and gut microbiota composition in normal and cyclophosphamide treated mice","volume":"9","author":"Tang","year":"2018","journal-title":"Food Funct."},{"key":"ref68","first-page":"235","article-title":"Analysis of carbohydrates by atmospheric pressure chloride anion attachment tandem mass spectrometry","volume-title":"Fuel","author":"Vinueza","year":"2013"},{"key":"ref69","doi-asserted-by":"publisher","first-page":"9116","DOI":"10.1073\/pnas.1632821100","article-title":"A chemical approach for identifying O-GlcNAc-modified proteins in cells","volume":"100","author":"Vocadlo","year":"2003","journal-title":"Proc. Natl. Acad. Sci. 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