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Investigation of Enzyme Immobilization and Clogging Mechanisms in the Enzymatic Synthesis of Amoxicillin.
Fan, Chenyan; Li, Jiale; Dong, Ruimeng; Xu, Yiling; Liu, Liqiang.
Affiliation
  • Fan C; College of Food and Biology, Hebei University of Science and Technology, Shijiazhuang 050018, China.
  • Li J; College of Food and Biology, Hebei University of Science and Technology, Shijiazhuang 050018, China.
  • Dong R; College of Food and Biology, Hebei University of Science and Technology, Shijiazhuang 050018, China.
  • Xu Y; College of Food and Biology, Hebei University of Science and Technology, Shijiazhuang 050018, China.
  • Liu L; College of Food and Biology, Hebei University of Science and Technology, Shijiazhuang 050018, China.
Int J Mol Sci ; 25(16)2024 Aug 06.
Article in En | MEDLINE | ID: mdl-39201244
ABSTRACT
This study investigated the blocking mechanism of immobilized penicillin G acylase (PGA) during the enzymatic synthesis of amoxicillin. Laboratory observations revealed that the primary cause of clogging was the crystallization of the substrate and product on the enzyme surface. Adjusting key parameters can significantly reduce clogging and improve catalytic efficiency. Methanol can decrease enzyme activity, but isopropyl alcohol cleaners can effectively remove clogs and protect enzyme activity. These findings provide an experimental foundation for optimizing the PGA immobilization process, which is crucial for achieving high efficiency and sustainability in industrial production.
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Full text: 1 Database: MEDLINE Main subject: Penicillin Amidase / Enzymes, Immobilized / Amoxicillin Language: En Year: 2024 Type: Article

Full text: 1 Database: MEDLINE Main subject: Penicillin Amidase / Enzymes, Immobilized / Amoxicillin Language: En Year: 2024 Type: Article