Theory of the kinetics of reactions catalyzed by enzymes attached to the interior surfaces of tubes | Zendy

Koyayashi Takeshi | Zendy; Laidler Keith J. | Zendy

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Theory of the kinetics of reactions catalyzed by enzymes attached to the interior surfaces of tubes

Author(s) -

Koyayashi Takeshi,

Laidler Keith J.

Publication year - 1974

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.260160108

Subject(s) - substrate (aquarium) , kinetics , product inhibition , chemistry , michaelis–menten kinetics , non competitive inhibition , catalysis , tube (container) , enzyme , product (mathematics) , enzyme kinetics , kinetic energy , reaction rate , thermodynamics , stereochemistry , materials science , organic chemistry , enzyme assay , mathematics , active site , physics , geometry , biology , composite material , classical mechanics , ecology

A theoretical treatment is given of the kinetics of reactions catalyzed by enzymes attached to the inner surface of a tube, through which the substrate solution passes. A utilization factor, the ratio of the actual reaction rate to that in the absence of diffusional effects, is defined. A numerical procedure is proposed and numerical and approximate solutions for the utilization factor are given for five kinetic conditions: (a) Michaelis‐Menten behavior, (b) substrate inhibition, (c) product inhibition (competitive), (d) product, inhibition (non‐competitive), and (e) product inhibition (anticompetitive). When the enzyme chemically attached to a tube obeys a Michaelis‐Menten relationship, criteria for insignificant and significant diffusional effects are proposed.

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