Biotechnology Letters

, Volume 21, Issue 11, pp 935–938

Localization and primary characterization of bile salt hydrolase from Lactobacillus reuteri

  • M.P. Taranto
  • F. Sesma
  • G. Font de Valdez
Article
  • 114 Downloads

Abstract

The bile salt hydrolase (BSH) of Lactobacillus reuteri CRL 1098 is a single, constitutive, intracellular enzyme which is only detectable in stationary phase cells. It has optimal activity at pH 4.5–5.5 and 37–45 °C. The enzyme (80 kDa apparent mass) has sulphydryl groups in the catalytic active site and hydrolyzes both glycine and taurine conjugated bile acids with higher affinity for glyco-conjugates.

bile salt hydrolase Lactobacillus reuten probiotic 

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Copyright information

© Kluwer Academic Publishers 1999

Authors and Affiliations

  • M.P. Taranto
    • 1
  • F. Sesma
    • 1
  • G. Font de Valdez
    • 1
  1. 1.Centro de Referencia para Lactobacilos (CERELA)CONICETS.M. de Tucumán

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