Novel Endo-β-N-Acetylglucosaminidases Derived from Human Fecal Samples Selectively Release N-Glycans from Model Glycoproteins

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dc.contributor.authorBolino, Matthew
dc.contributor.authorGamage, Nadini Haththotuwe
dc.contributor.authorDuman, Hatice
dc.contributor.authorAbiodun, Odunayo
dc.contributor.authorDe Mello, Amilton S.
dc.contributor.authorKarav, Sercan
dc.contributor.authorFrese, Steven A.
dc.date.accessioned2025-05-29T02:57:23Z
dc.date.available2025-05-29T02:57:23Z
dc.date.issued2025
dc.departmentÇanakkale Onsekiz Mart Üniversitesi
dc.description.abstractThree novel endo-beta-N-acetylglucosaminidases (AVUL01, BCAC01, and BFIN01) classified as members of the glucoside hydrolase (GH) family 18 were identified from human fecal samples and then cloned and characterized for their ability to hydrolyze two distinct classes of N-glycans. Endo-beta-N-acetylglucosaminidases (ENGases) are known for the hydrolysis of chitin and the N,N '-diacetylchitobiose core of N-linked glycans, depending on the glycan architecture. N-glycans have shown bioactivity as substrates in the human gut microbiome for microbes that encode ENGases, thus demonstrating their ecological relevance in the gut. However, distinct types of N-glycan structures, for example, oligomannosidic or complex, have been shown to enrich different microbes within the human gut. Novel advances in food technology have commercialized animal-derived dietary proteins with oligomannosidic instead of traditionally complex N-glycans using precision fermentation. This indicates that there is an unmet need to identify the classes of N-glycans that gut-derived ENGases act upon to determine whether these novel proteins alter gut ecology. AVUL01, BCAC01, and BFIN01 all demonstrated activity on exclusively oligomannosidic N-glycans from RNase B and bovine lactoferrin; however, they failed to show activity on complex or alpha-1,3-core fucosylated high-mannose N-glycans derived from fetuin and horseradish peroxidase, respectively. These results suggest that alpha-1,3 core fucosylation and complex N-glycan architecture inhibit the activity of AVUL01, BCAC01, and BFIN01. Furthermore, BFIN01 performed significantly better than BCAC01, resulting in a greater amount of N-glycans, suggesting that certain ENGases may possess enhanced specificity and kinetics as an evolutionary strategy to compete for resources.
dc.description.sponsorshipUniversity of Nevada, Reno Department of Nutrition, the College of Agriculture, Biotechnology, and Natural Resources, the Nevada Agriculture Experimental Station, and the Vice President for Research and Innovation; University of Nevada, Reno Department of Nutrition; Nevada Agriculture Experimental Station; Vice President for Research and Innovation [13385133]; New Investigator Seed Grant from the USDA National Institute of Food and Agriculture; Nevada INBRE [GM103440, GM104944]; NIGMS [P30GM145646]; National Institute of General Medical Sciences of the National Institutes of Health
dc.description.sponsorshipThis work was made possible by funding from the University of Nevada, Reno Department of Nutrition, the College of Agriculture, Biotechnology, and Natural Resources, the Nevada Agriculture Experimental Station, and the Vice President for Research and Innovation. This work was primarily supported by a New Investigator Seed Grant from the USDA National Institute of Food and Agriculture, #13385133. Funding was also received from Nevada INBRE via instrumentation and research awards provided by NIGMS (GM103440 and GM104944). Research reported in this publication was supported by the National Institute of General Medical Sciences of the National Institutes of Health under grant number P30GM145646.
dc.identifier.doi10.3390/foods14081288
dc.identifier.issn2304-8158
dc.identifier.issue8
dc.identifier.pmid40282690
dc.identifier.scopus2-s2.0-105003711317
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.3390/foods14081288
dc.identifier.urihttps://hdl.handle.net/20.500.12428/30040
dc.identifier.volume14
dc.identifier.wosWOS:001475072500001
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherMDPI
dc.relation.ispartofFoods
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_WOS_20250529
dc.subjectenzymes
dc.subjectgut microbiome
dc.subjectalternative protein
dc.subjectENGase
dc.subjectN-glycans
dc.titleNovel Endo-β-N-Acetylglucosaminidases Derived from Human Fecal Samples Selectively Release N-Glycans from Model Glycoproteins
dc.typeArticle

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