Thermal inactivation of immobilized penicillin acylase in the presence of substrate and products

Biotechnology and Bioengineering

Volumn 50, Issue 6, 1996, Pages 609-616

  Illanes, Andres ^a   Altamirano, Claudia ^a   Zuñiga, Maria Elvira ^a  

^a PONTIFICIA UNIVERSIDAD CATÓLICA DE VALPARAÍSO   (Chile)

Author keywords

6 aminopenicillanic acid; enzyme inactivation; penicillin acylase; product modulation; substrate modulation

Indexed keywords

AROMATIC COMPOUNDS; BIOREACTORS; CATALYSIS; ENZYME IMMOBILIZATION; MOLECULES; ORGANIC ACIDS; SUBSTRATES;

AMINOPENICILLANIC ACID; ENZYME DECAY; ENZYME INACTIVATION; ENZYME STABILITY; PENICILLIN ACYLASE; SUBSTRATE MODULATION; THERMAL INACTIVATION;

ENZYME KINETICS;

6 AMINOPENICILLANIC ACID; AMIDASE; BACTERIAL ENZYME; PENICILLIN G; PHENYLACETIC ACID;

ARTICLE; ENZYME IMMOBILIZATION; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME STABILITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; THERMOSTABILITY;

EID: 15844369202     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19960620)50:6<609::AID-BIT1>3.0.CO;2-O     Document Type: Article

References (47)

1. Alvaro, G., Fernández-Lafuente, R., Blanco, R., Guisán, J. M. Stabilizing effect of penicillin G sulfoxide, a competitive inhibitor of penicillin G acylase: its practical applications. 1991. Enzyme Microb. Technol. 13: 210-214.
2. Balasingham, K., Warburton, D., Dunnill, P., Lilly, M. D. 1972. The isolation and kinetics of penicillin amidase from Escherichia coli. Biochim. Biophys. Acta 26: 250-256.
3. Bickerstaff, G. 1984. Applications of immobilized enzymes to fundamental studies on enzyme structure and function, pp. 162-201. In: A. Wiseman (ed.), Topics in enzyme and fermentation biotechnology, vol. 9. Ellis Horwood, Chichester, UK.
4. Blanco, R. M., Guisán, J. M. Protecting effect of competitive inhibitors during very intense insolubilized enzyme-activated support multipoint attachments: trypsin (amine) agarose (aldehyde) system. 1988. Enzyme Microb. Technol. 10: 227-232.
5. Boehringer Mannheim 1993. Immobilized penicillin G amidase for the production of 6-aminopenicillanic acid and 7-aminodeacetoxy cephalosporanic acid. Catalogue no. 520-608.
6. Bourdillon, C., Thomas, V., Thomas, D. 1982. Electrochemical study of D-glucose oxidase autoinactivation. Enzyme Microb. Technol. 4: 175-180.
7. Bourdillon, C., Hervagault, C., Thomas, D. 1985. Increase in operational stability of immobilized glucose oxidase by the use of an artificial cosubstrate. Biotechnol. Bioeng. 27: 1619-1622.
8. Buchholz, K. 1982. Reaction engineering parameters for immobilized biocatalysts, pp. 39-71. In: A. Fiechter (ed.), Advances in biochemical engineering, vol. 24. Springer, Berlin.
9. Chen, K. C., Wu, J. Y. 1987. Substrate protection of immobilized glucose isomerase. Biotechnol. Bioeng. 30: 817-824.
10. Dagys, R., Pauliukonis, A., Kauzlauskas, D. 1984. New method for the determination of kinetic constants for two-stage deactivation of biocatalysts. Biotechnol. Bioeng. 26: 620-622.
11. Dordick, J. 1989. Enzymatic catalysis in monophasic organic solvents. Enzyme Microb. Technol. 11: 194-211.
12. Erarslan, A., Koçer, H. 1992. Thermal inactivation kinetics of penicillin G acylase obtained from a mutant derivative of Escherichia coli ATCC 11105. J. Chem. Technol. Biotechnol. 55: 79-84.
13. Greco, G., Veronese, F., Largajolli, R., Gianfreda, L. 1983. Purified penicillin acylase performance in a stabilized ultrafiltration membrane reactor. Eur. J. Appl. Microbiol. Biotechnol. 18: 33-38.
14. Greco, G., Pirozzi, D., Maremonti, M., Toscano, G., Gianfreda, L. 1993. The kinetics of enzyme deactivation, pp. 429-435. In: W. J. van den Tweel, A. Harder, and R. M. Buitelaar (eds.), Stability and stabilization of enzymes. Elsevier, Amsterdam.
15. Henley, J. P., Sadana, A. 1984. Series-type enzyme deactivations: influence of intermediate activity on deactivation kinetics. Enzyme Microb. Technol. 6: 35-41.
16. Henley, J. P., Sadana, A. 1985. Categorizations of enzyme deactivations using a series type mechanism. Enzyme Microb. Technol. 7: 50-60.
17. Henley, J. P., Sadana, A. 1986. Deactivation theory. Biotechnol. Bioeng. 28: 1277-1285.
18. Houng, J. Y., Yu, H. Y., Chen, K. C. 1993. Analysis of substrate protection of an immobilized glucose isomerase reactor. Biotechnol. Bioeng. 41: 451-458.
19. Illanes, A., Cartagena, O., Conejeros, R. 1992. Reactor design for penicillin acylase under thermal inactivation. In: Proceedings of the Ninth International Fermentation Symposium, Crystal City, VI, August 16-21.
20. Illanes, A., Acevedo, F., Gentina, J. C., Reyes, I., Torres, R., Cartagena, O., Ruiz, A., Vásquez, M. 1994. Production of penicillin acylase from Bacillus megaterium in complex and defined media. Proc. Biochem. 29: 263-270.
21. Illanes, A., Altamirano, C., Cartagena, O. 1994. Enzyme reactor performance under thermal inactivation, pp. 467-472. In: E. Galindo and O. T. Ramírez (eds.), Advances in bioprocess engineering. Kluwer, Dordrecht.
22. Ishimura, F., Seijo, H. 1991. Immobilization of penicillin acylase using porous polyacrylonitrile fibers. J. Ferment. Bioeng. 71: 140-143.
23. Ishimura, F., Suga, K. I. 1992. Hydrolysis of penicillin G by combination of penicillin acylase and electrodialysis. Biotechnol. Bioeng. 39: 171-175.
24. Katchalsky-Katzir, E. 1993. Immobilized enzymes - learning from past successes and failures. Trends Biotechnol. 11: 471-478.
25. Lee, Y., Fratzke, K., Wun, K., Tsao, G. 1976. Glucose isomerase immobilized on porous glass. Biotechnol. Bioeng. 18: 389-413.
26. Lee, S. B., Ryu, D. Y. 1982. Reaction kinetics and mechanisms of penicillin acylase: a comparative study by computer simulation. Enzyme Microb. Technol. 4: 35-38.
27. Lewis, Y., Humphrey, A. 1970. Optimal control of an enzyme reaction subject to enzyme deactivation. I. Batch process. Biotechnol. Bioeng. 12: 291-296.
28. Lin, C. 1986. An experimental method to determine the substrate protection of enzyme against decativation in a reversible reaction. Biochem. J. 16: 333-343.
29. Misset, O. 1993. Stability of industrial enzymes, pp. 111-131. In: W. J. van den Tweel, A. Harder, and R. M. Buitelaar (eds.), Stability and stabilization of enzymes. Elsevier, Amsterdam.
30. Naik, S., Karanth, N. 1978. Effect of internal and external diffusion on the apparent stability of immobilized enzyme catalysts. J. Appl. Chem. Biotechnol. 28: 569-580.
31. Niedermayer, A. 1964. Determination of phenylacetic acid in penicillin fermentation media by means of gas chromatography. Anal. Chem. 72: 248-254.
32. Noworyta, A., Bryjak, J. 1993. Process of penicillin G hydrolysis catalyzed by penicillin acylase immobilized on acrylic carrier. Bioproc. Eng. 9: 271-275.
33. O'Neill, S. 1972. Thermal inactivation of immobilized enzymes in ideal continuous reactors. Biotechnol. Bioeng. 14: 473-491.
34. Ospina, S., López-Munguía, A. González, R. L., Quintero, R. 1992. Characterization and use of a penicillin acylase biocatalyst. J. Chem. Technol. Biotechnol. 53: 205-214.
35. Park, J., Choi, C., Seong, B., Han, M. 1982. Effect of mass transfer in recirculation batch reactor system for immobilized penicillin amidase. Biotechnol. Bioeng. 24: 2215-2226.
36. Rodríguez, M., Quintero, R., López-Munguía, A. 1994. Design and kinetic characterization of a whole cell penicillin acylase biocatalyst using E. coli. Biotechnol. Bioeng. 29: 213-218.
37. Ryu, D., Bruno, C., Lee, B., Venkatasubramanian, K. 1972. Microbial penicillin amidohydrolase and the performance of a continuous enzyme reactor system, pp. 307-314. In: G. Terui (ed.), Fermentation technology today. Society of Fermentation Technology, Tokyo.
38. Sauber, K. 1993. Lessons from industry, pp. 145-151. In: W. J. van den Tweel, A. Harder, and R. M. Buitelaar (eds.), Stability and stabilization of enzymes. Elsevier, Amsterdam.
39. Self, D., Kay, G., Lilly, M. 1969. The conversion of benzylpenicillin to 6 aminopenicillanic acid using an insoluble derivative of penicillin amidase. Biotechnol. Bioeng. 11: 337-344.
40. Shami, E., Ramjeesingh, A., Rothstein, A., Zywulko, M. 1991. Stabilization of enzymes by their specific antibodies. Enzyme Microb. Technol. 13: 424-429.
41. Shewale, J., Kumar, K., Ambekar, G. 1987. Evaluation of determination of 6-amino penicillanic acid by p-dimethylaminobenzaldehyde. Biotechnol. Technics. 1: 69-72.
42. Shewale, J., Deshpande, S., Sudhakaran, V., Ambedkar, S. 1990. Penicillin acylase: applications and potentials. Proc. Biochem. 26: 97-103.
43. Valle, F., Balbás, P., Merino, E., Bolívar, F. 1991. The role of penicillin amidases in nature and in industry. Trends Biotechnol. 16: 36-41.
44. van den Tweel, W. J., Harder, A., Buitelaar, R. M. 1993. Stability and stabilization of enzymes. Elsevier, Amsterdam.
45. Villaume, I., Thomas, D., Legoy, M. D. 1990. Catalysis may increase the stability of an enzyme: the example of horse liver alcohol dehydrogenase. Enzyme Microb. Technol. 12: 506-509.
46. Volkin, D. B., Staubli, A., Langer, R., Klibanov, A. M. 1991. Enzyme thermoinactivation in anhydrous organic solvents. Biotechnol. Bioeng. 37: 843-853.
47. Warburton, D., Dunnill, P., Lilly, M. D. 1973. Conversion of benzylpenicillin to 6 aminopenicillanic acid in a batch reactor and continuous feed stirred tank reactor using immobilized penicillin amidase. Biotechnol. Bioeng. 15: 13-25.