Purification and characterisation of mannitol dehydrogenase from Lactobacillus sanfranciscensis.
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 degrees C, the pH optima for the reduction or oxidation were 5.8 and 8, respectively.
Korakli
Maher
M
Lehrstuhl für Technische Mikrobiologie, Technische Universität München, Weihenstephaner Steig 16, 85350 Freising, Germany. maher.korakli@wzw.tum.de
Vogel
Rudi F
RF
D000595:Amino Acid Sequence; D005632:Fructose / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007778:Lactobacillus / Q000145:classification / Q000201:enzymology* / Q000235:genetics; D008353:Mannitol / Q000378:metabolism; D008354:Mannitol Dehydrogenases / Q000302:isolation & purification / Q000378:metabolism*; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D010084:Oxidation-Reduction; D013696:Temperature
D008670:Metals; D005632:Fructose; D008353:Mannitol; D008354:Mannitol Dehydrogenases