Immobilisation of a 5′phosphodiesterase from vegetal origin by covalent binding on activated celite

Josep M. Serrat, M. Dolors Benaiges, Josep López-Santín

Research output: Contribution to journalArticleResearchpeer-review

Abstract

A vegetal enzyme, 5′phosphodiesterase, has been immobilised by covalent coupling onto activated Celite. This nonmicrobial activity was obtained from barley rootlets, an economical brewer's by-product. 5′ribonucleotides are selectively cleaved from RNA by a partially purified preparation of the enzyme. These compounds are high added value products used as flavor enhancers in food industries (disodium 5′inosinate, disodium 5′guanylate) and have important applications in the pharmaceutical industry (cytidine 5′phosphate, uridine 5′phosphate and adenine 5′phosphate). Glutaraldehyde was used as coupling agent. A concentration of 5 mM of glutaraldehyde was found adequate. Using a charge of 160.8 units μ g carrier-1 a total of 15% of the activity could be recovered in the carrier. The characterisation of the solid biocatalist is reported. © 1992 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.
Original languageEnglish
Pages (from-to)51-59
JournalBiocatalysis and Biotransformation
Volume6
Issue number1
DOIs
Publication statusPublished - 1 Jan 1992

Keywords

  • 5′phosphodiesterase
  • Celite
  • Glutaraldehyde
  • Immobilisation
  • Vegetal enzyme

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