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Backmixing and mass transfer in the design of immobilized‐enzyme reactors
Author(s) -
Kobayashi Takeshi,
MooYoung M.
Publication year - 1971
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.260130612
Subject(s) - mass transfer , chemistry , dispersion (optics) , piston (optics) , mixing (physics) , immobilized enzyme , michaelis–menten kinetics , reactor design , degree (music) , flow (mathematics) , chromatography , mechanics , enzyme , thermodynamics , enzyme assay , nuclear engineering , physics , organic chemistry , engineering , wavefront , quantum mechanics , acoustics , optics
The effects of dispersion and mass transfer resistance on the degree of conversion in an immobilized‐enzyme reactor have been considered theoretically. It is assumed that the immobilized enzymes obey a Michaelis–Menten relationship and backmixing can be characterized by a dispersion model. For two extreme cases (perfect mixing and piston flow), approximate equations are obtained, which can be readily used to evaluate the effect of mass transfer on degree of conversion. Numerical solutions are obtained for other intermediate cases. Design charts are given which set practical limits of enzyme reactor design.