The oxidation of 20 carbohydrates and derivatives by 45 strains of acetic acid bacteria, representing most of the known species, was studied and correlated with the enzymic constitution of the organisms. The strains of the mesoxydans group of Frateur and the acetate-oxidizing Gluconobacters oxidized the greatest variety of substrates and contained the most complex enzyme system. The strains inv...

The synthesis of cellulose by washed suspensions of Acetobatter xylinum proceeds in the presence of iodoacetate at concentrations which completely inhibit the oxidation of glyceraldehyde-a-phosphate (1). Since glucose was the only carbon compound added, the possibility was considered that the energy required for the biosynthetic process may be derived from reactions linked to the pentose phosph...

Acetobacter pasteurianus strains IFO3283, SKU1108, and MSU10 were grown under acetic acid fermentation conditions, and their growth behavior was examined together with their capacity for acetic acid resistance and pellicle formation. In the fermentation process, the cells became aggregated and covered by amorphous materials in the late-log and stationary phases, but dispersed again in the secon...

beta-Fructofuranosidases share a conserved aspartic acid-containing motif (Arg-Asp-Pro; RDP) which is absent from alpha-glucopyranosidases. The role of Asp-309 located in the RDP motif of levansucrase (EC 2.4.1.10) from Acetobacter diazotrophicus SRT4 was studied by site-directed mutagenesis. Substitution of Asp-309 by Asn did not affect enzyme secretion. The kcat of the mutant levansucrase was...

In this paper we construct spatially consistent second order explicit discretizations for time dependent hyperbolic problems, starting from a given Residual Distribution (RD) discrete approximation of the steady operator. We explore the properties of the RD mass matrices necessary to achieve consistency in space, and finally show how to make use of second order mass lumping to obtain second ord...

The recombinant fructosyltransferase (Ftf) of Streptococcus salivarius was expressed in Escherichia coli and purified to electrophoretic homogeneity after a combination of adsorption, ion-exchange and gel-filtration chromatography. The N-terminal signal sequence of the Ftf was removed by E. coli at the same site as in its natural host. The purified Ftf exhibited maximum activity at pH 6.0 and 3...