Enzymatic characterization of highly stable human alpha-galactosidase A displayed on magnetic particles

José L. Corchero; Rosa Mendoza; Neus Ferrer-Miralles; Anna Montràs; Lluís M. Martínez; Antonio Villaverde

doi:10.1016/j.bej.2012.05.003

Enzymatic characterization of highly stable human alpha-galactosidase A displayed on magnetic particles

José L. Corchero, Rosa Mendoza, Neus Ferrer-Miralles, Anna Montràs, Lluís M. Martínez, Antonio Villaverde

Department of Genetics and Microbiology

Research output: Contribution to journal › Article › Research › peer-review

10 Citations (Scopus)

Abstract

The human α-galactosidase A (EC 3.2.1.22, GLA), a lysosomal enzyme with important biotechnological and biomedical applications, has been successfully immobilized for the first time onto different versions of micro-sized magnetic particles by means of alternative coupling chemistries (covalent and metal affinity adsorption). The immobilized enzyme shows higher specific activity than its soluble counterpart and its enhanced stability as well as the magnetic-controlled positioning and reusability provided by coupling make these new bioconjugates excellent platforms for the presentation of highly active and pure versions of human GLA for both in vitro catalysis and therapeutic applications. © 2012 Elsevier B.V.

Original language	English
Pages (from-to)	20-27
Journal	Biochemical Engineering Journal
Volume	67
DOIs	https://doi.org/10.1016/j.bej.2012.05.003
Publication status	Published - 15 Aug 2012

Keywords

Biocatalysis
Enzyme activity
Human alpha-galactosidase A
Immobilized enzymes
Magnetic microparticles
Microcarriers
Operational stability

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10.1016/j.bej.2012.05.003

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title = "Enzymatic characterization of highly stable human alpha-galactosidase A displayed on magnetic particles",

abstract = "The human α-galactosidase A (EC 3.2.1.22, GLA), a lysosomal enzyme with important biotechnological and biomedical applications, has been successfully immobilized for the first time onto different versions of micro-sized magnetic particles by means of alternative coupling chemistries (covalent and metal affinity adsorption). The immobilized enzyme shows higher specific activity than its soluble counterpart and its enhanced stability as well as the magnetic-controlled positioning and reusability provided by coupling make these new bioconjugates excellent platforms for the presentation of highly active and pure versions of human GLA for both in vitro catalysis and therapeutic applications. {\textcopyright} 2012 Elsevier B.V.",

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doi = "10.1016/j.bej.2012.05.003",

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journal = "Biochemical Engineering Journal",

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T1 - Enzymatic characterization of highly stable human alpha-galactosidase A displayed on magnetic particles

AU - Corchero, José L.

AU - Mendoza, Rosa

AU - Ferrer-Miralles, Neus

AU - Montràs, Anna

AU - Martínez, Lluís M.

AU - Villaverde, Antonio

PY - 2012/8/15

Y1 - 2012/8/15

N2 - The human α-galactosidase A (EC 3.2.1.22, GLA), a lysosomal enzyme with important biotechnological and biomedical applications, has been successfully immobilized for the first time onto different versions of micro-sized magnetic particles by means of alternative coupling chemistries (covalent and metal affinity adsorption). The immobilized enzyme shows higher specific activity than its soluble counterpart and its enhanced stability as well as the magnetic-controlled positioning and reusability provided by coupling make these new bioconjugates excellent platforms for the presentation of highly active and pure versions of human GLA for both in vitro catalysis and therapeutic applications. © 2012 Elsevier B.V.

AB - The human α-galactosidase A (EC 3.2.1.22, GLA), a lysosomal enzyme with important biotechnological and biomedical applications, has been successfully immobilized for the first time onto different versions of micro-sized magnetic particles by means of alternative coupling chemistries (covalent and metal affinity adsorption). The immobilized enzyme shows higher specific activity than its soluble counterpart and its enhanced stability as well as the magnetic-controlled positioning and reusability provided by coupling make these new bioconjugates excellent platforms for the presentation of highly active and pure versions of human GLA for both in vitro catalysis and therapeutic applications. © 2012 Elsevier B.V.

KW - Biocatalysis

KW - Enzyme activity

KW - Human alpha-galactosidase A

KW - Immobilized enzymes

KW - Magnetic microparticles

KW - Microcarriers

KW - Operational stability

U2 - 10.1016/j.bej.2012.05.003

DO - 10.1016/j.bej.2012.05.003

M3 - Article

SN - 1369-703X

VL - 67

SP - 20

EP - 27

JO - Biochemical Engineering Journal

JF - Biochemical Engineering Journal

ER -

Enzymatic characterization of highly stable human alpha-galactosidase A displayed on magnetic particles

Abstract

Keywords

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