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Studies on lactate dehydrogenase of Lactobacillus plantarum spp. involved in lactic acid biosynthesis using permeabilized cells
Ist Teil von
Process biochemistry (1991), 2000-07, Vol.35 (10), p.1191-1198
Ort / Verlag
Elsevier Ltd
Erscheinungsjahr
2000
Quelle
Elsevier Journal Backfiles on ScienceDirect (DFG Nationallizenzen)
Beschreibungen/Notizen
Lactate dehydrogenase (LDH, EC 1.1.1.27) catalyses the reduction of pyruvate to lactate in facultative anaerobes. Whole cells of
Lactobacillus plantarum NCIM 2084 showed low levels of LDH activity but permeabilization of cells by treatment with organic solvents toluene, chloroform and diethyl ether increased the measurable LDH activities, ether treated cells showing the highest increase. The maximum intracellular activity was obtained upon treating the cells with ether (1%) at 28°C for 1 min. The LDH activity in permeabilized cells was nearly three-fold higher than that in the cell-free extract prepared by sonication. The kinetic properties of LDH in the permeabilized cells were comparable to that of cell-free extract, indicating that catalytically it functions similar to the isolated enzyme.