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CarBamate Kinase of Lactobacillus Buchneri Ncdo110. II. KInetic Studies and Reaction Mechanism
Biotechnology and Applied Biochemistry, 1987The participation of Mg2+ or Mn2+ nucleoside diphosphates in the reverse reaction catalyzed by purified carbamate kinase (ATP:carbamate phosphotransferase, EC 2.7.2.2) of Lactobacillus buchneri NCDO110 was studied. The results of initial velocity studies have indicated that Mn2+ ADP is as effective as a substrate as Mg2+ ADP is.
M C, Manca de Nadra +2 more
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[Bacteriocin properties of Lactobacillus fermenti, Lactobacillus brevis and Lactobacillus buchneri].
Antibiotiki, 1980Four bacteriocins of L. fermenti, 3 bacteriocins of L. brevis and 1 bacteriocin of L. buchneri were studied with respect to morphology of the inhibition growth zones of the indicator strains, capacity for diffusion through cellophane, sensitivity to high temperature, bacterial proteases, trypsin, chymotrypsin, pepsin, papain, nucleases and lysozyme ...
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The Silage Characteristics of Legume, grasses and Mixtures!of Siled with Lactobacillus Buchneri
2014The research was carried out to determine the effect of bacterial inoculant (Lactobacillus)buncheri) on the chemical composition!and the quality of the silages prepared from different forage crops and their mixtures. Sole silage of alfalfa, white clover, common vetch, soybean, chickpea, perinnal rygrass, wheat, triticale, oat and wild mustard ...
YÜCEL, C. +3 more
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Proteomic analyses of ethanol tolerance in Lactobacillus buchneri NRRL B‐30929
PROTEOMICS, 2014The Lactobacillus buchneri NRRL B‐30929 strain, isolated from a fuel ethanol (EtOH) production facility, exhibits high tolerance to environmental EtOH concentrations. This study aimed to identify proteins produced by B‐30929 in response to environmental EtOH.
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Carbamate kinase of Lactobacillus buchneri NCDO110. I. Purification and properties.
Biotechnology and applied biochemistry, 1987Carbamate kinase has been prepared from Lactobacillus buchneri NCDO110. An approximately 91-fold increase in the specific activity of the enzyme was achieved. The purified extract exhibited a single band following polyacrylamide gel electrophoresis. The apparent molecular weight as determined by gel electrophoresis was about 97,000.
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