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

Research output: Contribution to journalArticleResearchpeer-review

7 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 languageEnglish
Pages (from-to)20-27
JournalBiochemical Engineering Journal
Volume67
DOIs
Publication statusPublished - 15 Aug 2012

Keywords

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

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