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- Publisher
- Wiley
- Copyright
- Copyright © 1993 John Wiley & Sons, Inc.
- ISSN
- 0006-3592
- eISSN
- 1097-0290
- DOI
- 10.1002/bit.260410908
- pmid
- 18609637
- Publisher site
- See Article on Publisher Site
Abstract
10.1002/bit.260410908.abs The activity of bilirubin oxidase toward bilirubin was studied in a liquid/solid two‐phase low‐water organic system using a simple spectrophotometric assay to follow the reaction. The enzyme was lyophilized from aqueous solution before being suspended in the organic solvent reaction medium. The activity was significantly influenced by the properties of the aqueous medium from which the enzyme was lyophilized, specifically its pH, and the quantity and nature of the buffering species. Analyses of these effect showed that the role of buffering species in such systems went beyond their effect in fixing the protonation state of the enzyme. The activity was also influenced by the quantity of water added to the organic solvent reaction medium. The reaction was shown to follow Michaelis‐Menten Kinetics, and Km and kcat were determined. The liquid/solid two‐phase system studied was extensively compared to a previously studied water‐in‐oil microemulsion system © 1993 Wiley & Sons, Inc.
Journal
Biotechnology and Bioengineering – Wiley
Published: Apr 15, 1993