Mathematical determination of kinetic parameters for assessing the effect of the organic solvent on the selectivity of peptide synthesis with immobilized α-chymotrypsin

Carola Bahamondes, LORENA EVELYN WILSON SOTO, Fanny Guzmán, Andrés Illanes

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

The synthesis of the dipeptide N-benzoyl-L-tyrosine-L-argininamide (BTAA) was conducted under kinetic control with N-benzoyl-L-tyrosine ethyl ester as acyl donor and argininamide as nucleophile using immobilized α-chymotrypsin as catalyst. Using a mathematical procedure, the kinetic constants corresponding to the proposed mechanism of peptide synthesis were determined in three different cosolvent media, namely, ethanol, diglyme and acetonitrile. These constants were used for evaluating the selectivity of glyoxyl-agarose immobilized α-chymotrypsin in the synthesis of BTAA by determining the ratios of synthesis to hydrolysis rates.

Original languageEnglish
Pages (from-to)618-622
Number of pages5
JournalJournal of Bioscience and Bioengineering
Volume124
Issue number6
DOIs
StatePublished - Dec 2017
Externally publishedYes

Keywords

  • Enzyme mechanism
  • Kinetic control
  • Kyotorphin
  • Peptide synthesis
  • α-Chymotrypsin

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