The phagocidal action of oxidation products of natural and synthetic amines by crystalline amine oxidase preparations has been investigated with a large variety of bacteriophages. Oxidized spermine was shown to inactivate T3, T5, T7, MS2, ϕ80, λ (Escherichia coli); ε15, ε34 (Salmonella anatum); Al (Bacillus subtilis); P465, P468, Ap85, P4 (Brevibacterium lactofermentum); I128T (Pseudomonas glycinea), I2418 (Xanthomonas phaseoli) and PK66 (Streptomyces griseus). Phages of T2, T4, T6, ϕX174 (E. coli), P22 (S. anatum) and M2, SP10 (B. subtilis) was not inactivated. Essentially the similar activity was observed with the oxidation products of spermidine and synthetic polyamines analogous to spermine. The reduction of logarithmic titers of survival phages by the oxidized polyamines proceeded linearly with both incubation time and concentration of the oxidized polyamines. Then, it is conceivable that the inactivation of phages may be due to the interaction between oxidized polyamine and phagal nucleic acid.
Journal Article Glutaric Acid, a New Precursor of Biotin Biosynthesis Get access Koichi Ogata, Koichi Ogata Department of Agricultural Chemistry Kyoto University, Kyoto Search for other works by this author on: Oxford Academic Google Scholar Yoshikazu Izumi, Yoshikazu Izumi Department of Agricultural Chemistry Kyoto University, Kyoto Search for other works by this author on: Oxford Academic Google Scholar Yoshiki Tani Yoshiki Tani Department of Agricultural Chemistry Kyoto University, Kyoto Search for other works by this author on: Oxford Academic Google Scholar Agricultural and Biological Chemistry, Volume 34, Issue 12, 1 December 1970, Pages 1870–1871, https://doi.org/10.1080/00021369.1970.10859864 Published: 01 December 1970 Article history Received: 06 October 1970 Published: 01 December 1970
Metabolites from salicylic acid by microorganisms were investigated. About eighty strains of bacteria which were able to utilize salicylic acid as a sole source of carbon were isolated from soil and other natural sources. Among these bacteria, several strains produced a large amount of keto acids in the culture fluid during the cultivation. The acid was isolated from the culture fluid of strain K 102 in crystalline form. The crystal was identified as α-ketoglutaric acid by physicochemical methods. From the taxonomical studies, the isolated bacterial strains K 102 and K 362 were assumed to be Pseudomonas sp.
Journal Article A Microbial Synthesis of Panto-thenylalcohol 4′-Phosphate Get access Sakayu Shimizu, Sakayu Shimizu Department of Agricultural Chemistry, Kyoto University, Kyoto Search for other works by this author on: Oxford Academic Google Scholar Hazimu Morioka, Hazimu Morioka Department of Agricultural Chemistry, Kyoto University, Kyoto Search for other works by this author on: Oxford Academic Google Scholar Yoshiki Tani, Yoshiki Tani Department of Agricultural Chemistry, Kyoto University, Kyoto Search for other works by this author on: Oxford Academic Google Scholar Koichi Ogata Koichi Ogata Department of Agricultural Chemistry, Kyoto University, Kyoto deceased. Search for other works by this author on: Oxford Academic Google Scholar Agricultural and Biological Chemistry, Volume 42, Issue 4, 1 April 1978, Pages 889–890, https://doi.org/10.1080/00021369.1978.10863079 Published: 01 April 1978 Article history Received: 11 October 1977 Published: 01 April 1978
A taxonomic investigation was made on a soil bacterium, strain KT 104, isolated and demonstrated by Kameda et al. to produce an acylase, which hydrolyzes only the 1.-isomer of acetyl-DL-tryptophan yielding L-tryptophan.From its morphological, cultural ar~d physiological characteristics, this bacterium was concluded to belong to Genus Pseudomonas.Ten grams of wet cells from 750 ml of culture fluid, corresponding to 1.80 g. of dry cells, produced the theoretical quantity (5.1g.) of L-tryptophan in 11 of the reaction mixture when incubated under the conditions of pH 7.8 and 37°C, for 16 hr., with 5x102 .mol.(12.3g.) of acetyl-DL-tryptophan.By their physicochemical analyses and chemical behaviors, the scaly crystals obtained by recrystallization from 70 f ethanol were proved to be L-tryptophan.Enzymatic properties of this acylase found in the cell suspension are as follows : the optimum pH for the reaction is 7.0-'7.5;the optimum temperature for the 1 hr, reaction, 54°C; the optimum concentration of cobaltous ion for the activation of the enzyme, 10-3 4 mol, f 1, and the degree of maximum activation, 200 °o.When the optimum conditions are applied, the use of this bacterial acylase seems promising for the industrial production of L-tryptophan.
The production of biotin and bisnorbiotin from biotin diaminocarboxylic acid by the resting cell system of microorganisms was studied. It was found that the resting cells of Bacillus sphaericus convert biotin diaminocarboxylic acid into biotin, and the cells of Rhodotorula rubra potently convert it into bisnorbiotin through biotin. The conversion products from biotin diaminocarboxylic acid by these resting cell systems were chromatographically identified as biotin and bisnorbiotin. These conversions were markedly stimulated by addition of certain amino acids, especially alanine and glutamic acid, suggesting the important role of amino compound in the formation of ureido ring of biotin and bisnorbiotin molecules. This reaction occurred rather favorably under aerobic conditions.
Several conditions for the formation of coenzyme A from pantothenic acid and cysteine in the presence of ATP were investigated using Brevibacterium ammoniagenes IFO 12071 (A TCC 6871). The higher activity of the formation of coenzyme A was observed with the cells grown on acetate-medium. The effects of the substrate concentration, phosphate buffer concentration, pH and cell concentration on the formation of coenzyme A were examined and the amount of coenzyme A formed reached a maximum value of 1.2 mg per ml of the reaction mixture. Several surfactants belonging to cationics and anionics brought about 1.8-fold stimulation of the formation of coenzyme A. The considerable accumulation of coenzyme A in the culture broth during the growth was also observed.
