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Kinetics of bilirubin oxidase and modeling of an immobilized bilirubin oxidase reactor for bilirubin detoxification
Author(s) -
Million Claudy J. P.,
Klibanov Alexander M.,
Langer Robert
Publication year - 1988
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.260310605
Subject(s) - bilirubin , bilirubin oxidase , chemistry , albumin , chromatography , kinetics , biochemistry , enzyme , medicine , physics , quantum mechanics
Abstract The unbound bilirubin concentration and the enzymatic rate of bilirubin degradation by bilirubin oxidase in bilirubin‐serum albumin solutions have been investigated experimentally and theoretically. A stoichiometric bilirubin‐serum albumin binding analysis shows that the unbound bilirubin concentration depends only on the molar ratio of the total bilirubin concentration to the total serum albumin concentration. From the theoretical analysis and the measured unbound bilirubin concentrations, serum albumin may be modelled as a molecule having two binding sites, primary and secondary, with stoichiometric equilibrium constants of K 1 = 6 × 10 7 M −1 and K 2 = 4.5 × 10 6 M −1 , respectively. The rate of total bilirubin degradation in bilirubin‐serum albumin mixtures is zero order. An immobilized bilirubin oxidase reactor model, which shows good agreement with experimental bilirubin conversions, is presented. At a flow rate of 1 mL/min with a 8‐mL reactor volume, a 50% bilirubin conversion per pass was observed with an inlet bilirubin concentration of 350μ M and a serum albumin concentration of 500μ M .