Immobilization of β-galactosidase and α-mannosidase onto magnetic nanoparticles : A strategy for increasing the potentiality of valuable glycomic tools for glycosylation analysis and biological role determination of glycoconjugates

Dublin Core

Título

Immobilization of β-galactosidase and α-mannosidase onto magnetic nanoparticles : A strategy for increasing the potentiality of valuable glycomic tools for glycosylation analysis and biological role determination of glycoconjugates

Tema

INMOVILIZACION DE ENZIMAS
GLICOSIDASAS
ANALISIS GLICOMICO
BIBLIOGRAFIA NACIONAL QUIMICA
2018

Abstract

Glycans present in biological glycoconjugates have several structural and functional roles. Elucidation of glycan structure and biological function is critical to understand their role in physiological and pathogenic process, enabling the development of diagnostic methods and disease treatment. Immobilized glycosidases are powerful tools for glycan analysis, as they are able to remove specific carbohydrates without altering the protein structure. Here we describe the individual immobilization of Aspergillus oryzae β-galactosidase and Canavalia ensiformis α-mannosidase onto agarose and silica magnetic nanoparticles activated with cyanate ester groups. High immobilization yields (70–90%) were achieved, keeping above 60% of its original activity. Immobilized glycosidases were effective in the selective deglycosylation of model glycoproteins and a Fasciola hepatica lysate, evidenced by a decrease in specific lectin recognition of 40–50% after enzymatic deglycosylation. Immobilized glycosidases were reused for several deglycosylation cycles without loss of effectiveness. Their use was extended to the elucidation of the glycan role of native glycoconjugates. A decrease in the recognition of lactoferrin treated with α-mannosidase by a C-type lectin receptor, DC-SIGN was found. Also the specific deglycosylation of a F. hepatica lysate demonstrated the relevance of mannosylated glycans in the induction of Th2/Treg immune responses during the infection. Our results show successful immobilization of specific glycosidases in nano-supports and validate their utility to identify glycans biological functions.

Autor

Rodríguez, Ernesto
Francia, Karen.
Brossard, Natalie
García Vallejo, Juan J.
Kalay, Hakan
van Kooyk, Ivette
Freire, Teresa

Fuente

Enzyme and Microbial Technology  v. 117, 2018. --     p. 45-55

Editor

Elsevier

Fecha

2018

Derechos

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PDF

Idioma

Inglés

Tipo

Artículo

Identificador

DOI: 10.1016/j.enzmictec.2018.05.012

Document Item Type Metadata

Original Format

PDF
Fecha de agregación
November 5, 2018
Colección
Bibliografía Nacional Química
Tipo de Elemento
Document
Etiquetas
, ,
Citación
Rodríguez, Ernesto, “Immobilization of β-galactosidase and α-mannosidase onto magnetic nanoparticles : A strategy for increasing the potentiality of valuable glycomic tools for glycosylation analysis and biological role determination of glycoconjugates,” RIQUIM - Repositorio Institucional de la Facultad de Química - UdelaR, accessed November 14, 2018, http://riquim.fq.edu.uy/items/show/5338.
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