Modulation of penicillin acylase properties via immobilization techniques: one-pot chemoenzymatic synthesis of Cephamandole from Cephalosporin C.
The modulation of penicillin G acylase (PGA) properties via immobilization techniques has been performed studying the acylation of 7-aminocephalosporanic acid with R-mandelic acid methyl ester. PGA from Escherichia coli, immobilized onto agarose activated with glycidol (glyoxyl-agarose), has been used for the design of a novel one-pot synthesis of Cephamandole in aqueous medium and without isolation of intermediates, through three consecutive biotransformations catalyzed by D-amino acid oxidase, glutaryl acylase and PGA.
Terreni
M
M
Pharmaceutical Biocatalysis Laboratories, Dipartimento di Chimica Farmaceutica, Università degli Studi di Pavia, via Taramelli 12, 27100, Pavia, Italy. markt@pbl.unipv.it
Pagani
G
G
Ubiali
D
D
Fernández-Lafuente
R
R
Mateo
C
C
Guisán
J M
JM
D001671:Biochemistry / Q000379:methods*; D002435:Cefamandole / Q000138:chemical synthesis* / Q000378:metabolism; D002511:Cephalosporins / Q000737:chemistry* / Q000378:metabolism; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology; D010399:Penicillin Amidase / Q000737:chemistry* / Q000378:metabolism*; D012685:Sepharose / Q000737:chemistry
D002511:Cephalosporins; D004800:Enzymes, Immobilized; C025163:cephalosporin C; D002435:Cefamandole; D012685:Sepharose; D010399:Penicillin Amidase