Investigation of Enzyme Immobilization and Clogging Mechanisms in the Enzymatic Synthesis of Amoxicillin.
a blockage
amoxicillin
cleanse
enzymatic method
immobilized enzyme
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
06 Aug 2024
06 Aug 2024
Historique:
received:
21
06
2024
revised:
01
08
2024
accepted:
02
08
2024
medline:
31
8
2024
pubmed:
31
8
2024
entrez:
29
8
2024
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 39201244
pii: ijms25168557
doi: 10.3390/ijms25168557
pii:
doi:
Substances chimiques
Enzymes, Immobilized
0
Amoxicillin
804826J2HU
Penicillin Amidase
EC 3.5.1.11
Methanol
Y4S76JWI15
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM