Identification of an Escherichia coli periplasmic acid phosphatase containing of a 27 kDa-polypeptide component

Gian Maria Rossolini, Maria Cristina Thaller, Renato Pezzi, Giuseppe Satta

Research output: Contribution to journalArticle


An acid phosphatase containing a 27-kDa polypeptide component has been identified in Escherichia coli by means of a zymogram technique. The enzyme is secreted in the periplasmic space and is able to hydrolyze several organic phosphate esters, but not diesters, showing preferential activity on p-nitrophenyl phosphate and other phenolic phosphate esters. Production of the enzyme apparently occurs only in cells growing on carbon sources other than glucose.

Original languageEnglish
Pages (from-to)167-173
Number of pages7
JournalFEMS Microbiology Letters
Issue number1-2
Publication statusPublished - May 1 1994



  • Acid phosphatase
  • Escherichia coli

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Applied Microbiology and Biotechnology
  • Microbiology

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