Abstract:
:Thioredoxin (Trx1), a very important protein for regulating intracellular redox reactions, was immobilized on iron oxide superparamagnetic nanoparticles previously coated with 3-aminopropyltriethoxysilane (APTS) via covalent coupling using the EDC (1-ethyl-3-{3-dimethylaminopropyl}carbodiimide) method. The system was extensively characterized by atomic force microscopy, vibrational and magnetic techniques. In addition, gold nanoparticles were also employed to probe the exposed groups in the immobilized enzyme based on the SERS (surface enhanced Raman scattering) effect, confirming the accessibility of the cysteines residues at the catalytic site. For the single coated superparamagnetic nanoparticle, by monitoring the enzyme activity with the Ellman reagent, DTNB=5,5'-dithio-bis(2-15 nitrobenzoic acid), an inhibitory effect was observed after the first catalytic cycle. The inhibiting effect disappeared after the application of an additional silicate coating before the APTS treatment, reflecting a possible influence of unprotected iron-oxide sites in the redox kinetics. In contrast, the doubly coated system exhibited a normal in-vitro kinetic activity, allowing a good enzyme recovery and recyclability.
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
Netto CG,Nakamatsu EH,Netto LE,Novak MA,Zuin A,Nakamura M,Araki K,Toma HEdoi
10.1016/j.jinorgbio.2011.02.006subject
Has Abstractpub_date
2011-05-01 00:00:00pages
738-44issue
5eissn
0162-0134issn
1873-3344pii
S0162-0134(11)00035-3journal_volume
105pub_type
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