The effect of porosity on the catalytic performance of constant-mass, spherical beads containing immobilized enzyme

• Type: Article in International Scientific Journal
• Date: 1998

Authors

Cruz, IB (Author) Other; F. Xavier Malcata (Author) Other

Journal

Title: Bioprocess Engineering

Vol. 19 No. 6

Pages: 269-275

ISSN: 0178-515X

Publisher: Springer

Indexing

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Other information

Authenticus ID: P-001-6YQ

DOI: 10.1007/s004490050518

Abstract (EN): The mass balances to a spherical bead with increasing porosity, epsilon (obtained by plain expansion of an otherwise compact bead), containing an immobilized enzyme and surrounded by a stagnant film are developed in dimensionless form for the case of Michaelis-Menten kinetics by considering three alternative situations in terms of pore structure (either setting the pore number, the pore radius or the pore length as a constant). The pore pattern of the porous bead does not play a major role in the variation of the lowest concentration of substrate ever reached in the bulk of the bead, which increases as epsilon increases and eventually levels off when epsilon approaches unity. The ratio between the rate of reaction brought about by the immobilized enzyme within the porous bead and that obtained for a compact bead is greater when epsilon is higher, and a vertical asymptote is apparently reached when the porosity approaches unity, a trend that is similarly observed for all pore patterns considered.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 7