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Evaluation of the effectiveness factor along immobilized enzyme fixed‐bed reactors: Design of a reactor with naringinase covalently immobilized into glycophase‐coated porous glass
Author(s) -
Manjón A.,
Iborra J. L.,
Gómez J. L.,
Gómez E.,
Bastida J.,
Bódalo A.
Publication year - 1987
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/bit.260300405
Subject(s) - naringin , immobilized enzyme , porous glass , substrate (aquarium) , porosity , chemistry , kinetics , product inhibition , packed bed , diffusion , chemical engineering , chromatography , thermodynamics , enzyme , non competitive inhibition , organic chemistry , physics , oceanography , quantum mechanics , engineering , geology
A design equation is presented for packed‐bed reactors containing immobilized enzymes in spherical porous particles with internal diffusion effects and obeying reversible one‐intermediate Michaelis–Menten kinetics. The equation is also able to explain irreversible and competitive product inhibition kinetics. It allows the axial substrate profiles to be calculated and the dependence of the effectiveness factor along the reactor length to be continuously evaluated. The design equation was applied to explain the behavior of naringinase immobilized in Glycophase‐coated porous glass operating in a packed‐bed reactor and hydrolyzing both p ‐nitrophenyl‐α‐ L ‐rhamnoside and naringin. The theoretically predicted results were found to fit well with experimentally measured values.