Process Biochemistry, Год журнала: 2024, Номер unknown
Опубликована: Ноя. 1, 2024
Язык: Английский
Process Biochemistry, Год журнала: 2024, Номер unknown
Опубликована: Ноя. 1, 2024
Язык: Английский
Bioresource Technology, Год журнала: 2024, Номер 418, С. 131982 - 131982
Опубликована: Дек. 16, 2024
Язык: Английский
Процитировано
6Catalysts, Год журнала: 2024, Номер 14(12), С. 911 - 911
Опубликована: Дек. 11, 2024
Formolase, a thiamine pyrophosphate (TPP)-dependent enzyme, catalyzes the carboligation of three one-carbon formaldehyde molecules into one three-carbon dihydroxyacetone molecule. It has many important functions in biosynthesis carbon-based compounds and utilization CO2. However, enzyme low activity stability catalytic process, resulting high cost applications. To improve stability, formolase was immobilized onto magnetic nanoparticles, which were designed to have functional epoxy groups for covalently binding enzyme. In immobilization, effects pH, temperature, cofactor TPP on immobilization investigated optimized. The results showed that retention highly related TPP. presence TPP, specific 6.8 times higher than without optimal conditions as follows: temperature 20 °C, pH 7.0, an time 8 h, loading mg/g. Molecular docking used analyze effect stabilization indicated TTP could stabilize structure during immobilization. be reference other enzymes with cofactor.
Язык: Английский
Процитировано
1Biochemical Engineering Journal, Год журнала: 2024, Номер unknown, С. 109584 - 109584
Опубликована: Ноя. 1, 2024
Язык: Английский
Процитировано
0Process Biochemistry, Год журнала: 2024, Номер unknown
Опубликована: Ноя. 1, 2024
Язык: Английский
Процитировано
0