ISSN:
0178-515X
Source:
Springer Online Journal Archives 1860-2000
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Abstract The mass balances to a spherical bead with increasing porosity, ɛ (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 ɛ increases and eventually levels off when ɛ 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 ɛ 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s004490050518
Permalink
