Synthesis of the kyotorphin precursor benzoyl-L-tyrosine-L-argininamide with immobilized α-chymotrypsin in sequential batch with enzyme reactivation

Carola Bahamondes, Lorena Wilson, Claudia Bernal, Andrés Illanes, Gregorio Álvaro, Fanny Guzmán

Research output: Contribution to journalArticleResearchpeer-review

4 Citations (Scopus)

Abstract

© 2016 American Institute of Chemical Engineers. α-Chymotrypsin was immobilized in activated agarose support and the stability of the biocatalyst was assessed in three polar organic solvents, namely, ethanol, diglyme, and acetonitrile. Ethanol was the solvent in which the stability of the enzyme was higher and was then selected to perform the synthesis of the kyotorphin derivative benzoyl-tyrosine argininamide, evaluating enzyme reactivation after synthesis. Substrates for reaction were benzoyl tyrosine ethyl ester and argininamide, the reaction being performed under kinetic control. High conversion yield (85%) was obtained and the immobilized enzyme was successfully used in sequential batch reactor operation with enzyme reactivation after three batches.
Original languageEnglish
Pages (from-to)54-59
JournalBiotechnology Progress
Volume32
Issue number1
DOIs
Publication statusPublished - 1 Jan 2016

Keywords

  • Enzymatic reactivation
  • Enzymatic synthesis
  • Kyotorphin
  • α-chymotrypsin

Fingerprint Dive into the research topics of 'Synthesis of the kyotorphin precursor benzoyl-L-tyrosine-L-argininamide with immobilized α-chymotrypsin in sequential batch with enzyme reactivation'. Together they form a unique fingerprint.

Cite this