A copper(II) thiosemicarbazone complex built on gold for the immobilization of lipase and laccase

A self-assembled monolayer (SAM) of imidazole-2-carbaldehyde thiosemicarbazone (H2ImTSC) on gold was formed and characterized by ATR-FTIR, Time-of-Flight Secondary Ion Mass Spectrometry (ToF-SIMS) and X-ray Photoelectron Spectroscopy (XPS). The self-assembly of the ligand through its thioenolate group was confirmed by ToF-SIMS and the presence of XPS peaks at 161.9 (S2p1/2) and 163.1 eV (S2p3/2). The two nitrogen donor atoms of self-assembled HImTSC were able to coordinate (κ2-N,N) copper(II) when set to interact with a CuCl2 solution upon a second deprotonation of the ligand. This way, two types of modified gold sheets for the immobilization of lipase and laccase were obtained: (a) SAM of the ligand on gold (Au–HImTSC), and (b) SAM of HImTSC with a second monolayer of copper(II) (Au–ImTSC–Cu(II)). The highest immobilization of enzyme was achieved for laccase on Au–ImTSC–Cu(II) according to XPS and enzymatic activity determinations. Copper(II) played a an important recognition role through coordination to the enzyme and/or electrostatic interactions. Nevertheless, the positively charged surface of Au–ImTSC–Cu(II) affected the activity of laccase.

A copper(II) complex with imidazole-2-carbaldehyde thiosemicarbazone was built Layer-by-Layer on a gold surface for the immobilization of lipase and laccase.Figure optionsDownload high-quality image (102 K)Download as PowerPoint slide