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Resumo(s)
The mass balances to a spherical bead with increasing
porosity, e (obtained by plain expansion of an
otherwise compact bead), containing an immobilized enzyme
and surrounded by a stagnant ®lm 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 e increases
and eventually levels off when e 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 e 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.
Descrição
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Contexto Educativo
Citação
CRUZ, I. B.; MALCATA, F. X. - The effect of porosity on the catalytic performance of constant-mass, spherical beads containing immobilized enzyme. Bioprocess Engineering. ISSN 0178-515X. Vol. 19 (1998), p.269-275
Editora
Springer-Verlag