Investigation of Enzyme Immobilization and Clogging Mechanisms in the Enzymatic Synthesis of Amoxicillin

• Published in: International journal of molecular sciences Vol. 25; no. 16; p. 8557
• Main Authors: Fan, Chenyan, Li, Jiale, Dong, Ruimeng, Xu, Yiling, Liu, Liqiang
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 06.08.2024; MDPI
• Subjects: a blockage; Alcohol; amoxicillin; Amoxicillin - chemistry; Antibiotics; Biocatalysis; cleanse; Crystallization; Efficiency; Environmental protection; enzymatic method; Enzymes; Enzymes, Immobilized - chemistry; Enzymes, Immobilized - metabolism; immobilized enzyme; Investigations; Methanol - chemistry; Penicillin; Penicillin Amidase - chemistry; Penicillin Amidase - metabolism; Scanning electron microscopy; Sustainable development; Temperature; China; immobilized enzyme; amoxicillin; cleanse; a blockage; enzymatic method
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms25168557

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.