Wide-range and selective detection of SARS-CoV-2 DNA via surface modification of electrolyte-gated IGZO thin-film transistors.

The 2019 coronavirus pandemic resulted in a massive global healthcare crisis, highlighting the necessity to develop effective and reproducible platforms capable of rapidly and accurately detecting SARS-CoV-2. In this study, we developed an electrolyte-gated indium-gallium-zinc-oxide (IGZO) thin-film transistor with sequential surface modification to realize the low limit of detection (LoD <50 fM) and a wide detection range from 50 fM to 5 µM with good linearity (R2 = 0.9965), and recyclability. The surface chemical modification was achieved to anchor the single strand of SARS-CoV-2 DNA via selective hybridization. Moreover, the minute electrical signal change following the chemical modification was investigated by in-depth physicochemical analytical techniques. Finally, we demonstrate fully recyclable biosensors based on oxygen plasma treatment. Owing to its cost-effective fabrication, rapid detection at the single-molecule level, and low detection limit, the proposed biosensor can be used as a point-of-care platform to perform timely and effective SARS-CoV-2 detection.

Optimization of lactulose synthesis from whey lactose by immobilized ß-galactosidase and glucose isomerase.

In the present study, commercially available whey was used as a lactose source, and immobilized ß-galactosidase and glucose isomerase were used to synthesize lactulose from whey lactose in the absence of fructose. Optimal reaction conditions, such as lactose concentration, temperature, ionic strength of the buffer, and ratio of immobilized enzymes, were determined to improve lactulose synthesis using immobilized enzymes. Lactulose synthesis using immobilized enzymes improved markedly after optimizing the reaction conditions. When the lactulose synthesis was carried out at 53.5°C using 20% (w/v) whey lactose, 12U/ml of immobilized ß-galactosidase and 60U/ml of immobilized glucose isomerase in 100mM sodium phosphate buffer at pH 7.5, the lactulose concentration and specific productivity were 7.68g/l and 0.32mg/Uh, respectively. Additionally, when the immobilized enzymes were reused for lactulose synthesis, their catalytic activity was 57.1% after 7 repeated uses.