Recent advances in immobilization strategies for glycosidases

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dc.authoridbarile, daniela/0000-0002-3889-1596
dc.authoridKARAV, SERCAN/0000-0003-4056-1673
dc.contributor.authorKarav, Sercan
dc.contributor.authorCohen, Joshua L.
dc.contributor.authorBarile, Daniela
dc.contributor.authorde Moura Bell, Juliana Maria Leite Nobrega
dc.date.accessioned2025-01-27T20:47:27Z
dc.date.available2025-01-27T20:47:27Z
dc.date.issued2017
dc.departmentÇanakkale Onsekiz Mart Üniversitesi
dc.description.abstractGlycans play important biological roles in cell-to-cell interactions, protection against pathogens, as well as in proper protein folding and stability, and are thus interesting targets for scientists. Although their mechanisms of action have been widely investigated and hypothesized, their biological functions are not well understood due to the lack of deglycosylation methods for large-scale isolation of these compounds. Isolation of glycans in their native state is crucial for the investigation of their biological functions. However, current enzymatic and chemical deglycosylation techniques require harsh pretreatment and reaction conditions (high temperature and use of detergents) that hinder the isolation of native glycan structures. Indeed, the recent isolation of new endoglycosidases that are able to cleave a wider variety of linkages and efficiently hydrolyze native proteins has opened up the opportunity to elucidate the biological roles of a higher variety of glycans in their native state. As an example, our research group recently isolated a novel Endo--N-acetylglucosaminidase from Bifidobacterium longum subsp. infantis ATCC 15697 (EndoBI-1) that cleaves N-N-diacetyl chitobiose moieties found in the N-linked glycan (N-glycan) core of high mannose, hybrid, and complex N-glycans. This enzyme is also active on native proteins, which enables native glycan isolation, a key advantage when evaluating their biological activities. Efficient, stable, and economically viable enzymatic release of N-glycans requires the selection of appropriate immobilization strategies. In this review, we discuss the state-of-the-art of various immobilization techniques (physical adsorption, covalent binding, aggregation, and entrapment) for glycosidases, as well as their potential substrates and matrices. (c) 2016 American Institute of Chemical Engineers Biotechnol. Prog., 33:104-112, 2017
dc.description.sponsorshipNational Institutes of Health (Bethesda, MD) [R01AT007079, R01AT008759]; UC Davis Sustainable AgTech Innovation Center (Davis, CA); Center for Advanced Processing and Packaging Studies (CAPPS); Peter J. Shields Endowed Chair in Dairy Food Science (Davis, CA); Training Program in Biomolecular Technology at the University of California, Davis [T32-GM008799]
dc.description.sponsorshipThis research was supported in part by funding from the National Institutes of Health (Bethesda, MD) awards R01AT007079 and R01AT008759, the UC Davis Sustainable AgTech Innovation Center (Davis, CA), Center for Advanced Processing and Packaging Studies (CAPPS) and the Peter J. Shields Endowed Chair in Dairy Food Science (Davis, CA). This research was partially supported by an industry/campus supported fellowship under the Training Program in Biomolecular Technology (T32-GM008799) at the University of California, Davis.
dc.identifier.doi10.1002/btpr.2385
dc.identifier.endpage112
dc.identifier.issn8756-7938
dc.identifier.issn1520-6033
dc.identifier.issue1
dc.identifier.pmid27718339
dc.identifier.scopus2-s2.0-84996567208
dc.identifier.scopusqualityQ2
dc.identifier.startpage104
dc.identifier.urihttps://doi.org/10.1002/btpr.2385
dc.identifier.urihttps://hdl.handle.net/20.500.12428/24915
dc.identifier.volume33
dc.identifier.wosWOS:000394889400012
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherWiley
dc.relation.ispartofBiotechnology Progress
dc.relation.publicationcategoryinfo:eu-repo/semantics/openAccess
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_WoS_20250125
dc.subjectglycosidases
dc.subjectimmobilization
dc.subjectN-glycans
dc.subjectnutrition
dc.titleRecent advances in immobilization strategies for glycosidases
dc.typeReview Article

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