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(1976)
Scola - Nagelschneider and P . Hemmerich , Eur
- Publisher
- Wiley
- Copyright
- Copyright © 1979 John Wiley & Sons, Inc.
- ISSN
- 0006-3592
- eISSN
- 1097-0290
- DOI
- 10.1002/bit.260210909
- pmid
- 227492
- Publisher site
- See Article on Publisher Site
Abstract
10.1002/bit.260210909.abs Flavokinase (ATP: riboflavin 5'‐phosphotransferase, EC 2.7.1.26) purified from rat liver by affinity chromatography, has been immobilized by amide linkage to aminoalkyl‐agarose beads. The immobilized enzyme differs from the soluble enzyme in having greater stability slightly higher Km for the substrates, riboflavin and ATP, a broader pH optimum, and a lower energy of activation. These results suggest that the immobilized enzyme is influenced by the microenvironment of the bead and is subject to some degree of internal diffusional limitation. A Small (3ml), continuous, plug‐flow reactor prepared with immobilized flavokinase effects 5% conversion of riboflavin to riboflavin 5′‐phosphate (FMN) with a flow rate of 0.16 ml/min, which corresponds to an output of 5 nmol FMN/min. Immobilized flavokinase is effective for phosphorylating riboflavin and numerous riboflavin analogs and provides a facile methods for preparing exclusively, unlike other synthetic methods, the 5′‐phosphates.
Journal
Biotechnology and Bioengineering – Wiley
Published: Sep 1, 1979