A Specific Mannitol Dehydrogenase from Lactobacillus brevis

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Cloning, expression, purification, and analysis of mannitol dehydrogenase gene mtlK from Lactobacillus brevis.

The commercial production of mannitol involves high-pressure hydrogenation of fructose using a nickel catalyst, a costly process. Mannitol can be produced through fermentation by microorganisms. Currently, a few Lactobacillus strains are used to develop an efficient process for mannitol bioproduction; most of the strains produce mannitol from fructose with other products. An approach toward imp...

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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 re...

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Alcohol Dehydrogenase from Lactobacillus brevis: A Versatile Robust Catalyst for Enantioselective Transformations

The alcohol dehydrogenase from Lactobacillus brevis (LbADH) is a versatile catalyst for enantioselective reduction of ketones. Its substrate scope is wide with high regioand enantioselectivity. In this critical review, we have gathered the information available on the substrate scope as well as the applications reported. Quantitative information such as productivity per catalyst, space-time yie...

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Mannitol Dehydrogenase from Agaricus Campestris.

Enzymes capable of catalyzing n-mannitol formation from n-fructose or n-fructose 6-phosphate have been identified in various microorganisms. Substrate and coenzyme specificity have been established in only a few instances, but there appear to be enzymes, dependent upon nicotinamide adenine dinucleotide and upon nicotinamide adenine dinucleotide phosphate, which reduce fructose directly to manni...

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The pyruvate metabolism of LactobaciUus plantarum and Latobacillus arabino8su, which according to Bergey (1948) are identical organisms, has been studied by Rowatt (1951) and Nossal (1952). Both these homofermentative lactobacilli were shown to form 3-hydroxybutan-2-one (acetoin) as the main product of their pyruvate metabolism. No one appears to have studied the metabolism of pyruvate by any o...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1963

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)81106-1