A5004091697- Enzyme Catalysis and Immobilization
- Microbial Metabolic Engineering and Bioproduction
- Antibiotic Resistance in Bacteria
- Analytical Chemistry and Chromatography
- Enzyme Production and Characterization
- Pancreatic function and diabetes
- Electrochemical sensors and biosensors
- Pharmaceutical and Antibiotic Environmental Impacts
- Transgenic Plants and Applications
- Protein purification and stability
- Biotin and Related Studies
Sookmyung Women's University
2015-2022
Biodiesel and flavor compound production using enzymatic transesterification by microbial lipases provides mild reaction conditions low energy cost compared to the chemical process. SGNH-type are very effective catalysts for due their high rate, great stability, relatively small size convenient genetic manipulations, ease of immobilization. Hence, it is highly important identify novel with catalytic efficiencies good stabilities.A promiscuous cold-adapted lipase (HaSGNH1) from...
Bacterial hormone-sensitive lipases (bHSLs), which are homologous to the catalytic domains of human HSLs, have received great interest due their uses in preparation highly valuable biochemicals, such as drug intermediates or chiral building blocks. Here, a novel cold-active HSL from Halocynthiibacter arcticus (HaHSL) was examined and its enzymatic properties were investigated using several biochemical biophysical methods. Interestingly, HaHSL acted on large variety substrates including...
Molecular information about family VIII esterases, which have similarities with class C β-lactamases and penicillin-binding proteins, remains largely unknown. In this study, a novel esterase β-lactamase activity (PsEstA) from Paenibacillus sp. was characterized using several biochemical biophysical methods. PsEstA effective on broad range of substrates including tertiary butyl acetate, glyceryl tributyrate, glucose pentaacetate, olive oil, p-nitrophenyl esters. Additionally, hydrolyzed...