Recombinant Production and Characterization of a Novel ?-L-Fucosidase from Bifidobacterium castoris

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dc.authorid0000-0003-4566-8015
dc.authorid0000-0003-4056-1673
dc.contributor.authorPekdemir, Burcu
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.abstractalpha-L-fucosidases (EC 3.2.1.51) are of particular interest due to their ability to cleave terminal alpha-L-fucose residues from glycoconjugates, a property associated with numerous biological and therapeutic effects. They have also been investigated for their potential use in glycan remodeling, disease biomarker analysis, and particularly as therapeutic agents in the context of fucosidosis, a rare lysosomal storage disorder, caused by a deficiency in alpha-L-fucosidase activity. However, limitations in enzyme availability, stability, and substrate specificity highlight the need for novel and more efficient enzyme sources. Bifidobacterium castoris (B. castor is) is a newly identified species first discovered in the beaver gut microbiota in 2019. Phylogenetic studies have revealed its advanced metabolic capacity, and genomic analyses have demonstrated its extensive carbohydrate metabolism potential. This research article focuses on the recombinant production and biochemical characterization of a novel alpha-L-fucosidase from B. castoris LMG (Laboratorium voor Microbiologie Gent) 30937, predicted to belong to glycoside hydrolase family 29 (GH29) according to Universal Protein Resource (UniProt) annotation. Under optimized reaction conditions the recombinant alpha-L-fucosidase exhibited a specific activity of 0.264 U/mg to pNP-Fuc (4-Nitrophenyl-alpha-L-fucopyranoside). The results indicate that the enzyme is active in the pH range of 3.0-8.0 and temperatures of 24-42 degrees C, but its optimum conditions are the slightly acidic pH of 5.5 and the elevated temperature of 42 degrees C. This profile suggests that the enzyme is adapted to acidic intestinal-like environments. This novel enzyme expands the GH29 alpha-L-fucosidase repertoire and offers a promising new candidate for future biotechnological applications.
dc.identifier.doi10.3390/ijms26199344
dc.identifier.issn1661-6596
dc.identifier.issn1422-0067
dc.identifier.issue19
dc.identifier.pmid41096611
dc.identifier.scopus2-s2.0-105018893403
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.3390/ijms26199344
dc.identifier.urihttps://hdl.handle.net/20.500.12428/34458
dc.identifier.volume26
dc.identifier.wosWOS:001593631400001
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.subjectalpha-L-fucosidase
dc.subjectL-fucose
dc.subjectdefucosylation
dc.subjectrecombinant enzyme production
dc.titleRecombinant Production and Characterization of a Novel ?-L-Fucosidase from Bifidobacterium castoris
dc.typeArticle

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