Fabrication of functional biomolecular layer using recombinant technique for the bioelectronic device

Abstract

A novel immobilization method of blue copper protein azurin on a gold surface was developed without a chemical linker using recombinant technique. Azurin was recombined with a cysteine anchors by site-directed mutagenesis (SDM) and used to effect the mutations, changing the codon for Leu39Cys (L39C) from CTG to TGC. The immobilization of the functionalized protein is confirmed by surface plasmon resonance (SPR) and its surface morphology is analyzed by scanning tunneling microscopy (STM). The immobilization efficiency has been increased about 76.3%, as compared to that of wild type azurin. The electrochemical property of the fabricated thin film was investigated by cyclic voltammetry (CV). As a result, cysteine-modified azurin can be used for making high quality protein film, and applied to the fabrication of nano-scale bioelectronics.

Electrochemical biomemory device consisting of recombinant protein molecules

“…The protein characteristics need to be sustained after protein recombination. Usually, Escherichia coli bacteria are used to generate recombinant protein [88,89]. They regenerated recombinant azurin with cysteine residues by site mutagenesis and simple demonstration was illustrated in Fig.…”

Specificity of odorant-binding proteins: a factor influencing the sensitivity of olfactory receptor-based biosensors

“…Sensitivity is a highly important issue in the development of an effective biosensor [12][13][14]; thus, enormous efforts have been made to maximize sensitivity in various detection systems [15][16][17][18][19]. OBPs can be used to increase the sensitivity of olfactory receptor-based biosensors [20].…”