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

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 parame...

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Bibliographic Details
Published in:International journal of molecular sciences 2024-08, Vol.25 (16), p.8557
Main Authors: Fan, Chenyan, Li, Jiale, Dong, Ruimeng, Xu, Yiling, Liu, Liqiang
Format: Article
Language:English
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
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Summary: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.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms25168557