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Easily handling penicillin G acylase magnetic cross-linked enzymes aggregates: Catalytic and morphological studies

Paper ID Volume ID Publish Year Pages File Format Full-Text
34821 45051 2014 9 PDF Available
Title
Easily handling penicillin G acylase magnetic cross-linked enzymes aggregates: Catalytic and morphological studies
Abstract

•Magnetic-CLEAs (M-CLEAs) were prepared using PGA as enzyme model.•M-CLEAs and CLEAs morphological structures and catalytic properties were compared.•M-CLEAs magnetic recovery and reuse were perfect.

Biomolecules labeled with superparamagnetic nanoparticles can be selectively removed from complex reaction mixtures using an external magnetic field. Amino-functionalized superparamagnetic iron oxide nanoparticles (amino-SPION) were co-aggregated with penicillin G acylase and then cross-linked, generating magnetic cross-linked enzymes aggregates (M-CLEAs) that were quickly and efficiently recovered from the reaction medium by applying an external magnetic field. M-CLEAs and cross-linked enzymes aggregates (CLEAs) prepared under the same reaction conditions were characterized and compared. The best recovered activities were obtained for M-CLEAs prepared using polyethylene glycol 600 as precipitant and the most stable M-CLEA were obtained using tert-butanol. Successive penicillin G hydrolysis reactions were carried out using the same M-CLEA in a 50 mL reactor (3 reaction cycles), after the reactions the derivate was magnetically recovered without loss of activity demonstrating a total magnetic recovery. Line-scan energy dispersive X-ray spectroscopy showed that the amino-SPIONs were homogeneously dispersed within the structure of the M-CLEA.

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Keywords
Cross-linked enzymes aggregates; Superparamagnetic nanoparticles; Supramolecular complex; Magnetic recovery of enzymes; Penicillin hydrolysis
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Easily handling penicillin G acylase magnetic cross-linked enzymes aggregates: Catalytic and morphological studies
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 49, Issue 1, January 2014, Pages 38–46
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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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
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