Purification and characterisation of mannitol dehydrogenase from Lactobacillus sanfranciscensis

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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. © 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

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Korakli, M., & Vogel, R. F. (2003). Purification and characterisation of mannitol dehydrogenase from Lactobacillus sanfranciscensis. FEMS Microbiology Letters, 220(2), 281–286. https://doi.org/10.1016/S0378-1097(03)00129-0

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