Purification and characterisation of mannitol dehydrogenase from Lactobacillus sanfranciscensis

Maher Korakli, Rudi F. Vogel

Research output: Contribution to journalArticlepeer-review

40 Scopus citations

Abstract

Mannitol dehydrogenase (MDH) was purified and characterised from Lactobacillus sanfranciscensis. Two peptide fragments of MDH were N-terminally sequenced for the first time in the genus Lactobacillus. The purified enzyme had an apparent molecular mass of 44 kDa and catalysed both the reduction of fructose to mannitol and the oxidation of mannitol to fructose. The Km value for the reduction reaction was 24 mM fructose and that for the oxidation 78 mM mannitol. The optimum temperature was 35°C, the pH optima for the reduction or oxidation were 5.8 and 8, respectively.

Original languageEnglish
Pages (from-to)281-286
Number of pages6
JournalFEMS Microbiology Letters
Volume220
Issue number2
DOIs
StatePublished - 28 Mar 2003

Keywords

  • Mannitol dehydrogenase from Lactobacillus sanfranciscensis

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