Article Abstract:
Lactobacillus brevis and L. buchneri produce a 1,3-propanediol:NAD+ oxidoreductase which has properties similar to that of the corresponding Kleibsiella pneumoniae enzyme. Characterization of this enzyme showed that it is an octameric protein with molecular mass of 330 kDa, and requires manganous or ferrous ions for activity. It differs from the K pneuminiae enzyme in that it can dehydrogenate glycerol at a significant rate.In addition to glycerol, the enzyme is < 10% active with ethanol and 1,3- propanediol. These properties are markedly different from those of a L.reuteri 1,3-propanediol dehydrogenase.
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Article Abstract:
Microbial adhesion to solvents (MATS) methods and microelectrophoresis were utilized to characterize the hydrophilic and electrostatic cell properties of eight Lactobacillus (L.) strains. Physicochemical analysis of the cell surface properties of strains belonging to L. casei subsp. casei, L. paracasei subsp. paracasei and L. rhamnosus indicated the hydrophilic property of their cell surfaces. The L. strains also exhibited similar physicochemical properties due to identical cell surface architectures.
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Article Abstract:
The inhibitory effects of myoglobin on four aminopeptidases and one tripeptidase purified from Lactobacillus sake were investigated. Muscle myoglobin was added to a reaction mixture to determine the impact of myoglobin concentration levels on enzyme activity. Results showed that an increase in myoglobin results in a corresponding increase in inhibition of aminopeptidases. On the other hand, tripeptidase activity is not affected by myoglobin concentration.
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