fevereiro 2015 vol. 1 num. 2 - XX Congresso Brasileiro de Engenharia Química
Artigo - Open Access.
GREEN ROUTE FOR AMOXICILLIN PRODUCTION THROUGH THE INTEGRATION WITH THE RECYCLE OF THE BY-PRODUCT (P-HYDROXYPHENYLGLYCINE)
In the kinetically-controlled enzymatic synthesis of amoxicillin catalyzed by penicillin G acylase (PGA, E.C.18.104.22.168) p-hydroxyphenylglycine (PHPG) is a by-product continuously formed in the reaction. Also, methyl ester is the standard substrate used in the production of amoxicillin generating methanol as a by-product. Thus, we assessed the recovery and reuse of PHPG as reactant for the synthesis of p-hydroxyphenylglycine ethyl ester substrate (PHPGEE) and the integration to the process through the recycle of PHPGEE for the reactor of enzymatic synthesis of amoxicillin generating ethanol as a by-product. Recovery of the by-product of the enzymatic synthesis of amoxicillin was effective reaching a purity of 99% for the PHPG. Purified PHPG was successfully employed in the production of PHPGEE with a conversion of 93%. The enzymatic synthesis of amoxicillin employing the previously synthesized PHPGEE was feasible following the characteristic profile that is expected for these reactions.
-  CALLERI, E. et al. Penicillin G acylase-based stationary phases: analytical applications. J. Pharm. Biomed. Anal., v. 35, p. 243-258, 2004.
-  COLE, M. Penicillins and other acylamino compounds synthesized by cell-bound penicillin acylase of Escherichia coli. Biochem. J., v. 115, p. 747-756, 1969.
-  DIENDER, M. B. et al. Feasibility of the thermodynamically controlled synthesis of amoxicillin. J. Mol. Catal. B: Enzym., v. 5, p. 249-253, 1998.
-  FERNÁNDEZ-LAFUENTE, R. et al. Synthesis of antibiotics (cephaloglycin) catalyzed by penicillin G acylase: Evaluation and optimization of different synthetic approaches. Enzyme Microb. Technol., v. 19, p. 9-14, 1996.
-  GIORDANO, R. C.; RIBEIRO, M. P. A.; GIORDANO, R. L. C. Kinetics of β-lactam antibiotics synthesis by penicillin G acylase (PGA) from the viewpoint of the industrial enzymatic reactor optimization. Biotechnol. Adv., v. 24, p. 27-41, 2006.
-  MARGOLIN, A. L.; SVEDAS, V. K.; BEREZIN, I. V. Substrate-specificity of penicillin amidase from Escherichia coli. Biochim. Biophys. Acta, v. 616, p. 283-289, 1980.
-  PARMAR A. et al. Advances in enzymatic transformation of penicillins to 6-aminopenicillanic acid (6-APA). Biotechnol. Adv., v. 18, p. 289-301, 2000.
-  Área temática: Processos Biotecnológicos 7ROLINSON, G. N.; GEDDES, A. M. The 50th anniversary of the discovery of 6-aminopenicillanic acid (6-APA). Int. J. Antimicrob. Agents., v. 29, p. 3-8, 2007.
-  6. ACKNOWLEDGEMENTS The authors would like to thank Brazilian research-funding agencies (CAPES, CNPq and FAPESP) and the group of the Prof. Guisán (Department of Enzymatic Biocatalysis, Institute of Catalysis, CSIC, Madrid, Spain) for the biocatalyst.
PEREIRA, S. C.; CASTRAL, T. C.; RIBEIRO, M. P. A.; GIORDANO, R. L. C.; GIORDANO, R. C.; "GREEN ROUTE FOR AMOXICILLIN PRODUCTION THROUGH THE INTEGRATION WITH THE RECYCLE OF THE BY-PRODUCT (P-HYDROXYPHENYLGLYCINE)", p. 1823-1830 . In: Anais do XX Congresso Brasileiro de Engenharia Química - COBEQ 2014 [= Blucher Chemical Engineering Proceedings, v.1, n.2].
São Paulo: Blucher,
ISSN 2359-1757, DOI 10.5151/chemeng-cobeq2014-1263-20189-138533
últimos 30 dias | último ano | desde a publicação