Mathematical model for internal pH control in immobilized enzyme particles
article
A mathematical model has been developed for the internal pH control in immobilized enzyme particles. This model describes the kinetics of a coupled system of two enzymes, immobilized in particles of either planar, cylindrical, or spherical shape. The enzyme kinetics are assumed to be of a mixed type, including Michaelis-Menten kinetics, uncompetitive substrate inhibition, and competitive and noncompetitive product inhibition. As a case study the enzyme combination is considered urease and penicillin acylase, whose kinetics are coupled through the pH dependence of the kinetic parameters. The results of the computer simulations indicate that a high conversion of Pen-G may be achieved (80-90%) at bulk pH values of about 7. 5-8.
Topics
TNO Identifier
230173
ISSN
00063592
Source
Biotechnology and Bioengineering, 28(10), pp. 1582-1589.
Pages
1582-1589
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