Exploring the Activity of a Novel N-Glycosidase (EndoBI-2): Recombinant Production to Release Bioactive Glycans

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dc.authorid0000-0003-4056-1673
dc.contributor.authorDuman, Hatice
dc.contributor.authorAvci, Izzet
dc.contributor.authorSalih, Bekir
dc.contributor.authorKayili, Haci Mehmet
dc.contributor.authorBechelany, Mikhael
dc.contributor.authorKarav, Sercan
dc.date.accessioned2026-02-03T11:59:59Z
dc.date.available2026-02-03T11:59:59Z
dc.date.issued2025
dc.departmentÇanakkale Onsekiz Mart Üniversitesi
dc.description.abstractThe gut microbiome evolves in response to host development, health state, lifestyle, nutrition, and microbial interactions. The survival of gut microbiota depends on its ability to utilize its host-indigestible complex oligosaccharides. Certain gut microbes produce glycosidases that cleave N-glycoproteins to release N-glycans that are then used as a carbon source. However, commercial glycosidases are inefficient and, thus, require improved deglycosylation strategies to study their functions and scale up their production. Therefore, the main objective of this study was to recombinantly produce and characterize the novel endo-beta-N-acetylglucosaminidase 2 (EndoBI-2) from Bifidobacterium longum subsp. infantis (B. infantis) and to evaluate its enzymatic performance for controlled N-glycan release. Furthermore, the optimum reaction conditions for EndoBI-2 were investigated on model glycoprotein RNAse B using model glycoprotein. The released N-glycans were profiled by hydrophilic interaction liquid chromatography-fluorescence detection-quadrupole time-of-flight tandem mass spectrometry (HILIC-FLD-QTOF-MS/MS). We demonstrated that EndoBI-2 possesses a strong temperature tolerance and efficiently cleaves N-glycans under mild reaction conditions, exhibiting high activity at pH 5. These findings highlight EndoBI-2 as a robust and efficient biocatalyst for the production of bioactive N-glycans from diverse N-glycoproteins, with potential applications in glycobiotechnology.
dc.identifier.doi10.3390/ijms27010339
dc.identifier.issn1661-6596
dc.identifier.issn1422-0067
dc.identifier.issue1
dc.identifier.pmid41516219
dc.identifier.scopus2-s2.0-105026988989
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.3390/ijms27010339
dc.identifier.urihttps://hdl.handle.net/20.500.12428/34451
dc.identifier.volume27
dc.identifier.wosWOS:001657371300001
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherMdpi
dc.relation.ispartofInternational Journal of Molecular Sciences
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_WOS_20260130
dc.subjectendo-beta-N-acetylglucosaminidase
dc.subjectglycan profiling
dc.subjectglycoprotein
dc.subjectdeglycosylation
dc.subjectglycobiotechnology
dc.subjectmass spectrometry
dc.titleExploring the Activity of a Novel N-Glycosidase (EndoBI-2): Recombinant Production to Release Bioactive Glycans
dc.typeArticle

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