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Thermal inactivation of immobilized penicillin acylase in the presence of substrate and products
Author(s) -
Illanes Andres,
Altamirano Claudia,
Zuñiga Maria Elvira
Publication year - 1996
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19960620)50:6<609::aid-bit1>3.0.co;2-o
Subject(s) - substrate (aquarium) , penicillin , chemistry , penicillin amidase , substrate specificity , enzyme , microbiology and biotechnology , biochemistry , antibiotics , biology , ecology
Inactivation of immobilized penicillin acylase has been studied in the presence of substrate (penicillin G) and products (phenylacetic acid and 6‐aminopenicillanic acid), under the hypothesis that substances which interact with the enzyme molecule during catalysis will have an effect on enzyme stability. The kinetics of immobilized penicillin acylase inactivation was a multistage process, decay constants being evaluated for the free‐enzyme and enzyme complexes, from whose values modulation factors were determined for the effectors in each enzyme complex at each stage. 6‐Aminopenicillanic acid and penicillin G stabilized the enzyme in the first stage of decay. Modulation factors in that stage were 0.96 for penicillin G and 0.98 for 6‐aminopenicillanic acid. Phenylacetic acid increased the rate of inactivation in both stages, modulating factors being −2.31 and −2.23, respectively. Modulation factors influence enzyme performance in a reactor and are useful parameters for a proper evaluation. © 1996 John Wiley & Sons, Inc.