Penicillin acylase catalyzed synthesis of penicillin-G from substrates anchored in cyclodextrins.
Indian J Biochem Biophys
;
2000 Feb; 37(1): 6-12
Artículo
en Inglés
| IMSEAR
| ID: sea-26407
ABSTRACT
Penicillin acylase (EC 3.5.1.11) catalyses the condensation of phenylacetic acid (PAA) and 6-aminopenicillanic acid (6-APA) to form benzylpenicillin (BP). Both PAA and 6-APA were found to form host-guest complexes with beta-methylcyclodextrin (beta m-CD) and gamma-cyclodextrin (gamma-CD) respectively. The rate of the reaction catalyzed by the enzyme remained unaffected if one of the substrates used was in the cyclodextrin complexed form. However, in this case, the reaction lasted longer and yielded about 20 per cent more products compared to the condensation reaction involving only uncomplexed substrates. There was distinct increase in the rate of formation of the antibiotic, if both substrates used are in CD-complexed form.
Texto completo:
Disponible
Índice:
IMSEAR (Asia Sudoriental)
Asunto principal:
Penicilina G
/
Penicilina Amidasa
/
Fenilacetatos
/
Especificidad por Sustrato
/
Carbohidratos
/
Ácido Penicilánico
/
Ciclodextrinas
Idioma:
Inglés
Revista:
Indian J Biochem Biophys
Año:
2000
Tipo del documento:
Artículo
Similares
MEDLINE
...
LILACS
LIS