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- W1994598083 abstract "Abstract A second aminopeptidase was purified from cell-free extracts of Lactobacillus delbrueckii subsp. bulgaricus B14 by ammonium sulphate precipitation and two steps of anion-exchange chromatography. After SDS polyacrylamide-gel electrophoresis in the presence of β-mercaptoethanol, one protein band was detected at 54 kDa. The same molecular mass was estimated by gel filtration. SDS polyacrylamide-gel electrophoresis in the absence of β-mercaptoethanol resulted in a single band at 220 kDa, indicating that the enzyme forms complexes of four molecules under non-reducing conditions. Activity was markedly increased by reducing and metal-chelating agents. Thiol-group inhibitors, such as iodoacetic acid, inhibited the enzyme strongly. In contrast to Mg 2+ and Ca 2+ , which had slightly activating effects, other divalent cations reduced enzyme activity at a concentration of 1 mM. The aminopeptidase showed highest activity at 50°C and pH 6·5–7 and hydrolyzed a wide range of di- and tripeptides. The most suitable substrates were Leu-Gly, Leu-Gly-Gly, Ala-Ala-Ala, and Met-Gly-Gly. For Leu-Gly and Leu-Gly-Gly, K m - values of 1·81 mM and 2·17 mM and turnover numbers of 870 s −1 were calculated, with a maximal rate of hydrolysis ( V max ) of 4600 and 2780 μmol/min per mg of protein, respectively. The aminopeptidase did not cleave Lys-pNA, a substrate hydrolyzed by all type-‘N’ aminopeptidases from lactic acid bacteria with high velocities. It compared well, however, with pepC found in Lactococcus ." @default.
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- W1994598083 date "1993-01-01" @default.
- W1994598083 modified "2023-10-02" @default.
- W1994598083 title "Purification and characterization of a second aminopeptidase (pepC-like) from Lactobacillus delbrueckii subsp. bulgaricus B14" @default.
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- W1994598083 doi "https://doi.org/10.1016/0958-6946(93)90083-c" @default.
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