Studies on papain action in the synthesis of Gly-Phe in two-liquid-phase media

Josep Anton Feliu, Carles de Mas, Josep López-Santín

Research output: Contribution to journalArticleResearchpeer-review

22 Citations (Scopus)

Abstract

The synthesis of the protected dipeptide BocGly-PheOMe has been carried out in an aqueous-organic two-liquid-phase system. The reaction has been catalyzed by the protease papain using trichloroethylene as organic phase with an organic phase-aqueous phase volume ratio, Vorg Vaq, of 4. The results of the present article can be summarized as follows: a) A relationship between enzyme deactivation, interfacial area, and interfacial tension is stated. The addition of 0.4% Tween 80 to the reaction system stabilized papain activity for > 50 h, overcoming the problems related to the presence of the organic solvent and shear stress due to mixing; b) undesirable parallel reactions are identified; c) the peptide yield was increased by working with a fed-batch strategy. © 1995.
Original languageEnglish
Pages (from-to)882-887
JournalEnzyme and Microbial Technology
Volume17
Issue number10
DOIs
Publication statusPublished - 1 Jan 1995

Keywords

  • effect of interphase on enzymes
  • enzyme stability
  • Papain
  • peptide synthesis
  • two-liquid-phase system

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