Der Abbau von Phenylamiden durch Bacillus sphaericus

Zusammenfassung Die Acylanilide Monalide, Carboxin, Oxycarboxin, 2,5-Dimethylfurancarbonsäureanilid, Pyracarbolid, 2-Methyl- und 2-Chlorbenzoesäureanilid, der N-Phenylcarbaminsäureester Propham und die N-Phenylharnstoff-derivate Monolinuron, Linuron, Metobromuron und Maloran wurden durch B. sphaericus an der Amidbindung zu den entsprechenden Anilinen und Säuren gespalten.Der qualitative Nachweis der Zwischenprodukte gelang dünnschicht- und gaschromatographisch mit Hilfe von Vergleichssubstanzen.Für den Abbau der Phenylamide durch B. sphaericus wurde ein Abbauschema aufgestellt.

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The degradation of phenylamides by Bacillus sphaericus

Summary B. sphaericus is degrading the acylamides monalide, carboxin, oxycarboxin, 2,5-dimethylfurancarboxylic acid anilide, pyracarbolid, 2-methyl-and 2-chloro-benzoic acid anilide, the N-phenylcarbamate propham and the N-methoxyphenylurea compounds monolinuron, linuron, metabromuron and maloran by cleaving the amide linkage, forming the corresponding anilines and acids.The metabolites were determined qualitatively by the means of co-thinlayer- and co-gaschromatography.A pathway for degradation of the phenylamides by B. sphaericus is proposed.

     

Ammonium assimilation in Proteus vulgaris,Bacillus pasteurii,and Sporosarcina ureae

No active uptake of ammonium was detected in Proteus vulgaris, Bacillus pasteurii, and Sporosarcina ureae, which indicates that these bacteria depend on the passive diffusion of ammonia across the cell membrane. In P. vulgaris the glutamine synthetase-glutamate synthase (GS-GOGAT) pathway and glutamate dehydrogenase (GDH) were present, and these enzymes exhibited high affinities for ammonium. In B. pasteurii and S. ureae, however, no GS activity was detected, and GOGAT activity was only present in S. ureae. GDH enzymes were present in these two organisms, but showed only low affinity for ammonium, with apparent K _m-values of 55.2 mM in B. pasteurii and 36.7 mM in S. ureae, repectively. These observations explain why P. vulgaris is able to grow at neutral pH and low ammonium concentration (2 mM), while B. pasteurii and S. ureae require high ammonium concentration (40 mM) and alkaline pH for growth.Non-standard abbreviations GS glutamine synthetase - GOGAT glutamate synthase - GDH glutamate dehydrogenase - GT glutamyl transferase - MA methylammonium - NB nutrient broth - YE yeast extract - NA nocotinic acid     

l-Asparaginase from Proteus vulgaris

To produce an immunologically and enzymologically new type of l-asparaginase, 108 strains of bacteria were screened for enzyme production. As a result, 13 bacteria belonging to the genera Alcaligenes, Bacterium, and Proteus were found to produce l-asparaginases in high levels. Among these l-asparaginases, partially purified l-asparaginases from B. cadaveris and P. vulgaris showed antitumor activity. A partially purified l-asparaginase preparation of P. vulgaris did not react with the antibody of Escherichia colil-asparaginase on the Ouchterlony agar plate. Culture conditions for the production of l-asparaginase by P. vulgaris were investigated in detail. The enzyme was produced in high yields when cells were grown aerobically in a medium containing sodium fumarate and corn steep liquor. The addition of glucose or ammonium ion to the medium, however, resulted in depressed production of l-asparaginase. Under the optimum conditions, 3,700 international units of l-asparaginase was obtained from 1 liter of culture medium.     

Steuerung von Wachstum und Formbildung durch Wirkstoffe

Ohne ZusammenfassungMit Unterstützung der Deutschen Forschungsgemeinschaft, des Kultusministeriums und des Wirtschaftsministeriums des Landes Nordrhein-Westfalen.Herrn Prof. Dr. W. v.Buddenbrock zur Erreichung des 70. Lebensjahres gewidmet.     

Steuerung von Wachstum und Formbildung durch Wirkstoffe

Ohne ZusammenfassungMit UnterstÜtzung der Deutschen Forschungsgemeinschaft und des Kultusministeriums des Landes Nordrhein-Westfalen.     

Joint culturing of Streptococcus lactis, strain MGU with Proteus vulgaris and Bacillus mesentericus

Nisin synthesis by Streptococcus lactis, strain MGU, grown as a combined culture together with Proteus vulgaris and Bacillus mesentericus under stationary conditions or with stirring does not depend on the quantity of inoculated associated cells. Nisin synthesis in the combined culture drops down by 10-20% at the initial pH 7.5 of the growth medium which is unfavourable for S. lactis producing nisin. The level of nisin biosynthesis does not rise when the pH of the medium is adjusted (either naturally or artificially) to 6.6-6.8 in the presence of glucose and yeast autolysate. S. lactis inhibits the growth of B. mesentericus when grown together with it whereas P. vulgaris inhibits the growth of S. lactis in their combined culture.     

Isolation of Phenylalanine-Negative Proteus vulgaris

Three phenylalanine-negative Proteus vulgaris strains were isolated from three different sources. The significance of these Proteus strains has not been fully recognized.     

Bacteriophage Typing of Proteus mirabilis, Proteus vulgaris, and Proteus morganii

A bacteriphage typing scheme for differentiating Proteus isolated from clinical specimens was developed. Twenty-one distinct patterns of lysis were seen when 15 bacteriophages isolated on 8 Proteus mirabilis, 1 P. vulgaris, and 1 P. morganii were used to type 162 of 189 (85.7%) P. mirabilis and P. vulgaris isolates. Seven phages isolated on 3 P. morganii were used to type 13 of 19 (68.4%) P. morganii isolates. Overall, 84.1% of the 208 isolates were lysed by at least 1 phage at routine test dilution (RTD) or 1,000 x RTD. Fifty isolates, retyped several weeks after the initial testing, showed no changes in lytic patterns. The phages retained their titers after storage at 4 C for several months. A computer analysis of the data showed that there was no relationship between the source of the isolate and bacteriophage type. This bacteriophage typing system may provide epidemiological information on strains involved in human infections.     

Lecithinase activity of Proteus vulgaris

Lecithinase production is described as a new biochemical property of P. vulgaris strains grown in a selective agar medium containing brilliant green, crystal violet and lecithin (BCL agar), the authors' own modification of egg-yolk culture medium. By using this BCL agar as a medium inhibiting the swarming growth of P. vulgaris cultures the authors succeeded in identifying 12 lecithinase-positive strains among the P. vulgaris isolates obtained from patients with Crohn's disease. Of 50 P. mirabilis strains tested in parallel none gave the positive test for lecithinase production in this medium.     

Terminale und subterminale Oxidation von n-Alkanen durch Schimmelpilze

Zusammenfassung Der Abbau von n-Alkanen durch cunninghamella echinulata, Absidia glauca und Mucor sp. erfolgt durch monoterminale Oxidation ohne Freisetzung von primären oder sekundären Alkoholen, Ketonen und Aldehyden. Das Fettsäuremuster der cellulären Lipide zeigt eine deutliche Abhängigkeit vom gegebenen n-Alkan. Aspergillus-, Penicillium- und Verticillium-Arten oxidieren n-Alkane subterminal unter Bildung verschiedener isomerer sekundärer Alkohole und Ketone. Das Fettsäuremuster zeigt keine deutliche Abhängigkeit vom gegebenen n-Alkan. —Die Abbauwege werden diskutiert.

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Terminal and subterminal oxidation of n-alkanes by molds

Summary Degradation of n-alkanes by Cunninghamella echinulata, Absidia glauca and Mucor sp. is effected by monoterminal oxidation of the alkane chain and production of a cellular fatty-acid pattern that depends on the given n-alkane. Primary and secondary alcohols, ketones and aldehydes were not excreted in course of the oxidation. Subterminal attack on the alkane chain is found in members of the genus Aspergillus, Penicillium and Verticillium with the concomitant release of various isomeric secondary alcohols and ketones, and production of a cellular fatty-acid pattern which does not clearly depend on the given n-alkane. — The degradation pathways are discussed.

     

Sporulation-associated activation of Bacillus sphaericus larvicide

Preparations of the larvicidal crystal from 46-h cultures of Bacillus sphaericus 2362 contain 125-, 110-, 63-, and 43-kilodalton (kDa) proteins (P. Baumann, B. M. Unterman, L. Baumann, A.H. Broadwell, S.J. Abbene, and R.D. Bowditch, J. Bacteriol. 163:738-747, 1985). The 63- and 43-kDa proteins, which have been purified, are not immunologically cross-reactive, and only the 43-kDa protein is toxic to mosquito larvae. Since antigenic determinants of the two smaller proteins have been detected in the higher-molecular-weight proteins (125 and 110 kDa), it has been suggested that the latter are precursors of the 43- and 63-kDa peptides. In the present study, purified 110-kDa protein was found to be toxic to the larvae of Culex pipiens (50% lethal concentration = 115 ng/ml). A luciferase-luciferin assay for intracellular ATP as well as an assay based on the exclusion of Trypan Blue by live cells indicated that the 110-kDa protein had no effect on tissue-culture-grown cells of C. quinquefasciatus, while cells exposed to the 43-kDa protein rapidly lost viability (50% lethal concentration = 54 microgram(s)/ml by the intracellular ATP assay). These findings suggested that the 110-kDa protein and, by extension, the 125-kDa protein are protoxins which are activated during sporulation by cleavage to a 43-kDa toxin. To further investigate the origins and relationships of the crystal proteins of B. sphaericus, we analyzed samples during the growth and sporulation of the culture. Synthesis of crystal proteins was initiated at the end of exponential growth and was completed after about 7 h.(ABSTRACT TRUNCATED AT 250 WORDS)     

Progesterone side-chain cleavage by Bacillus sphaericus

The side-chain of progesterone was cleaved by Bacillus sphaericus to produce two C-19 keto androstene steroids. The structures of these metabolites were androstenedione and 1-dehydroandrostenedione. High concentrations of glucose in the culture medium inhibited conversion of progesterone to these two metabolites.