Open AccessPurification and characterisation of mannitol dehydrogenase from Lactobacillus sanfranciscensis
Author(s) -
Korakli Maher,
Vogel Rudi F
Publication year - 2003
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/s0378-1097(03)00129-0
Subject(s) - mannitol , fructose , biochemistry , dehydrogenase , lactate dehydrogenase , chemistry , enzyme , chromatography , biology
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 K m 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.