Article Abstract:
Research was conducted to examine two enzymes released by wild-type Leuconostoc mesenteroides NRRL B-1299 when grown in media devoid of sucrose. The two enzymes, glucose glycosyltransferase (GGT) and fructose glucosyltransferase (FGT), are produced at a lower level than extracellular dextransucrase sucrose glucosyltransferase produced on traditional culture mediums containing sucrose. Structural analysis of the dextran afforded from sucrose and of the oligosaccharides synthesized by acceptor reaction suggest that GGT and FGT are two new different enzymes.
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Article Abstract:
Leuconostoc mesenteroides NRRL B-512F dextransucrase is responsible for the synthesis of soluble dextran from sucrose precursors. The function of the carboxy terminal of this enzyme is investigated by creating three mutants with variable deletions in the carboxy terminal. Analysis of the activity of the mutant enzymes revealed that the carboxy terminal regulates the velocity of the reaction. Other enzyme parameters such as catalysis, Km and optimum pH, are unaffected by the deletions.
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Article Abstract:
The metabolic and energetic characteristics of Leuconostoc mesenteroides were studied to better understand the factors which affect dextransucrase activity and therefore permit the development of techniques for enhanced dextransucrase production. Glucose and fructose support equivalent specific growth rates under aerobic conditions, but glucose allows a better biomass yield in anaerobiosis. Sucrose supports a higher growth rate than the monosaccharides.
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