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Immobilization of the acylase from Escherichia coli on glyoxyl-agarose gives efficient catalyst for the synthesis of cephalosporins

Paper ID Volume ID Publish Year Pages File Format Full-Text
18412 42722 2008 9 PDF Available
Title
Immobilization of the acylase from Escherichia coli on glyoxyl-agarose gives efficient catalyst for the synthesis of cephalosporins
Abstract

The catalytic properties of penicillin G acylase (PGA) from Escherichia coli, when used in kinetically controlled N-acylation (kcNa) of cephalosporanic nuclei, can be strongly influenced by the moiety in 3-position of the cephem structure. In the synthesis of Cefonicid (1c), the adsorption of the cephalosporanic nucleus (7-SACA) in the PGA active site appeared sensitively increased by a positive ionic interaction between an arginine (ArgA145) in the enzyme active site and the sulphonic group of the β-lactam structure. Interestingly, when PGA was immobilized on solid supports, any effect depending on the substrate structure resulted minimized; the catalytic properties of this enzyme were affected with different outcomes depending on the type of matrix and binding chemistry. The PGA immobilized on glyoxyl-agarose (hydrophilic support activated with aldehyde groups) resulted in a good catalyst when used in kinetically controlled N-acylation of different cephalosporanic nuclei. This derivatives allow much better Vs/Vh1 (defined as the ratio between the rate of synthesis and the rate of hydrolysis of the acylating agent) than the same enzyme immobilized on Eupergit C, an acrylic hydrophobic supports activated with epoxy groups. The synthetic performances of the Eupergit derivative versus different nuclei were always much poorer if compared with glyoxyl-agarose or the soluble protein. The use of PGA immobilized on glyoxyl-agarose allowed the development of efficient processes for the preparation of Cefazolin in high yield and purity. The results obtained in the optimization of this process are presented.

Keywords
Immobilization; Enzyme catalysis; Acylation; Cephalosporins
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Immobilization of the acylase from Escherichia coli on glyoxyl-agarose gives efficient catalyst for the synthesis of cephalosporins
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 42, Issue 2, January 2008, Pages 121–129
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us