Nonionic tensides modify papain structure and proteolytic activity

M. Szögyi, T. Cserháti

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The effect of 33 polyethoxylated nonionic tensides with various hydrophobic moieties was studied on the proteolytic activity and phase transition behaviour of papain. Tensides with longer ethyleneoxide chain markedly increased the phase transition temperatures of papain indicating possible hydrogen bond formation between the hydrophilic ethyleneoxide chain and the polar substructures of papain. The character of lipophilic moiety of tensides influences also each physicochemical parameter of papain suggesting the existence of hydrophobic interactions too. The significant positive linear correlations between the activity increasing and structure stabilizing effects of tensides make probably that the structure modification of papain accounts for its enchanced proteolytic activity.

Original languageEnglish
Pages (from-to)85-92
Number of pages8
JournalActa Biotechnologica
Volume10
Issue number1
DOIs
Publication statusPublished - 1990

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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