Biophysical Chemistry, Journal Year: 2022, Volume and Issue: 292, P. 106915 - 106915
Published: Oct. 27, 2022
Language: Английский
Biophysical Chemistry, Journal Year: 2022, Volume and Issue: 292, P. 106915 - 106915
Published: Oct. 27, 2022
Language: Английский
Biochemical Engineering Journal, Journal Year: 2022, Volume and Issue: 185, P. 108524 - 108524
Published: June 23, 2022
Language: Английский
Citations
9Proteins Structure Function and Bioinformatics, Journal Year: 2023, Volume and Issue: 92(2), P. 170 - 178
Published: Sept. 27, 2023
Abstract Due to its bioactivity and versatile applications, levan has appeared as a promising biomaterial. Levansucrase is responsible for the conversion of sucrose into levan. With goal enhancing production, strategy stability levansucrase being intensively studied. To make proteins more stable under high temperatures, proline, most rigid residue, can be introduced previously flexible regions. Herein, G249, D250, N251, H252 on coil close calcium binding site Bacillus licheniformis were replaced with proline. Mutations at G249P greatly enhance both enzyme's thermodynamic kinetic stability, while those H252P improve solely stability. GPC analysis revealed that synthesize levan, but generate primarily oligosaccharides. Molecular dynamics simulations (MD) MM/GBSA mutation increased not only levansucrase, also affinity toward fructan.
Language: Английский
Citations
5World Journal of Microbiology and Biotechnology, Journal Year: 2022, Volume and Issue: 38(9)
Published: July 1, 2022
Language: Английский
Citations
8Biophysical Chemistry, Journal Year: 2022, Volume and Issue: 292, P. 106915 - 106915
Published: Oct. 27, 2022
Language: Английский
Citations
1