Purification and covalent immobilization of benzaldehyde lyase with heterofunctional chelate-epoxy modified magnetic nanoparticles and its carboligation reactivity
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Tarih
2013
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Elsevier Science Bv
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
In this work, histidine-tagged recombinant benzaldehyde lyase from Pseudomonas fluorescens Biovar I (BAL, EC 4.1.2.38) was immobilized on the magnetically responsive epoxy-chelate magnetic support following a two-step mechanism; that is, the protein is physically adsorbed and then the covalent bonding takes place. This mechanism has been exploited to combine the selectivity of metal chelate affinity chromatography with the covalent immobilization capacity of epoxy supports. In this way, it has been possible to accomplish, in a simple manner, the purification, immobilization, and stabilization of a histidine-tagged recombinant benzaldehyde lyase. To fulfill this objective we prepared and characterized a multifunctional Co2+-IDA-epoxy functionalized the silica coated magnetic nanoparticles (SCMPs) which are modified with glycidyloxypropyltrimethoxysilane (GPTMS) and iminodiacetic acid (IDA). To test immobilized BAL, benzoin condensation reaction was performed with this magnetically responsive biocatalyst. The results obtained from the carboligation reaction that was performed with this simple and convenient heterogeneous biocatalyst were comparable to that of free-enzyme-catalyzed reaction. Additional advantages are its reusability and it is easy to work with. (c) 2013 Elsevier B.V. All rights reserved.
Açıklama
Anahtar Kelimeler
Immobilized Benzaldehyde Lyase, Epoxy-Chelate Magnetic Support, Metal-Affinity Magnetic Nanoparticles, Selective Immobilization, Multipoint Covalent Attachment, One Step Purification
Kaynak
Journal of Molecular Catalysis B-Enzymatic
WoS Q Değeri
Q2
Scopus Q Değeri
N/A
Cilt
95
