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

Paper ID Volume ID Publish Year Pages File Format Full-Text
3499 173 2012 8 PDF Available
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.

► The human α-galactosidase A enzyme has been coated onto magnetic microparticles. ► His-tag directed anchoring results in better performance than covalent conjugation. ► Immobilized enzyme shows better activity and stability than the soluble form. ► Coating onto magnetic carriers allows the recycling of the immobilized catalyst.

Keywords
Immobilized enzymes; Human alpha-galactosidase A; Magnetic microparticles; Biocatalysis; Microcarriers; Enzyme activity; Operational stability
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Enzymatic characterization of highly stable human alpha-galactosidase A displayed on magnetic particles
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 67, 15 August 2012, Pages 20–27
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us