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Bacillus subtilis

The rat LD qS are 13, 3.6 (oral) and 21, 6.8 (dermal) mg/kg. Parathion is resistant to aqueous hydrolysis, but is hydroly2ed by alkah to form the noninsecticidal diethjlphosphorothioic acid and -nitrophenol. The time required for 50% hydrolysis is 120 d ia a saturated aqueous solution, or 8 h ia a solution of lime water. At temperatures above 130°C, parathion slowly isomerizes to 0,%diethyl 0-(4-nitrophenyl) phosphorothioate [597-88-6] which is much less stable and less effective as an insecticide. Parathion is readily reduced, eg, by bacillus subtilis ia polluted water and ia the mammalian mmen to nontoxic 0,0-diethyl 0-(4-aminophenyl) phosphorothioate, and is oxidized with difficulty to the highly toxic paraoxon [511-45-5] diethyl 4-nitrophenyl phosphate d 1.268, soluble ia water to 2.4 mg/L), rat oral LD q 1.2 mg/kg. [Pg.282]

Fig. 1. Enzymatic liquefaction processes (9). Alpha-S is the a-amylase from bacillus subtilis alpha-L/ST are a-amylases from B. licheniformis oi B. Fig. 1. Enzymatic liquefaction processes (9). Alpha-S is the a-amylase from bacillus subtilis alpha-L/ST are a-amylases from B. licheniformis oi B.
Further efficient fermentative methods for manufacture of riboflavin have been patented one is culturing C. famata by restricting the carbon source uptake rate, thereby restricting growth in a linear manner by restriction of a micronutrient. By this method, productivity was increased to >0.17 g riboflavin/L/h (63). The other method, using Bacillus subtilis AJ 12644 low in guanosine monophosphate hydrolase activity, yielded cmde riboflavin 0.9 g/ L/3 days, when cultured in a medium including soy protein, salts, and amino acids (64). [Pg.78]

Ethylene oxide is able to inactivate all microorganisms. Bacterial spores are more resistant than vegetative cells, yeasts, and molds (287). Spores are 5 to 10 times more resistant than the vegetative cells (288). bacillus subtilis spores were the most resistant of those tested (289). Ethylene oxide was also shown to be vimcidal (290). [Pg.138]

A number of steroids have been regioselectively acylated ia a similar manner (99,104). Chromobactenum viscosum hpase esterifies 5a-androstane-3P,17P-diol [571-20-0] (75) with 2,2,2-triduoroethyl butyrate ia acetone with high selectivity. The hpase acylates exclusively the hydroxy group ia the 3-position giving the 3P-(monobutyryl ester) of (75) ia 83% yield. In contrast, bacillus subtilis protease (subtihsia) displays a marked preference for the C-17 hydroxyl. Candida iylindracea]i 2Lse (CCL) suspended ia anhydrous benzene regioselectively acylates the 3a-hydroxyl group of several bile acid derivatives (104). [Pg.342]

Another unusual rearrangement is performed by Bacillus subtilis during the catabolism of sepiapterin (237), in converting the whole side-chain with subsequent oxidation of the pyrazine ring into 6-(l-carboxyethoxy)pterin (238 equation 75). [Pg.309]

Tricyclic pyrazole derivatives (698) are described by Hashem et al. as inhibitors of the growth of Bacillus subtilis, Pseudomonas fluorescens, Staphylococcus aureus and KB cells at moderate concentrations (76JMC229). [Pg.294]

Subtilisin (from Bacillus subtilis) [9014-01-1 ] [EC 3.4.21.62]. Purified by affinity chromatography using 4-(4-aminophenylazo)phenylarsonic acid complex to activated CH-Sepharose 4B. [Chandraskaren and Dhai Anal Biochem 150 141 7955]. [Pg.568]

Bacillus subtilis (B. Subtilis) An aerobic bacterium used as a host in rDNA experiments. [Pg.900]

Bacillus subtilis RNase RNA b Where 3 -P04 is to purine oligos with purine 3 -P04 ends... [Pg.349]

Alkaline protease from Bacillus subtilis DY, pH 8, 37°, 80-85% yield. Methyl esters are cleaved similarly. [Pg.418]

A subsequent patent, U.S. Patent 2,828,246 described a commercial process for bacitracin production. A 1,230 gallon portion of a medium containing 10% soybean oil meal, 2.50% starch and 0.50% calcium carbonate having a pH of 7.0 was inoculated with a culture of bacitracin-producing bacteria of the Bacillus subtilis group and the inoculated medium incubated for a period of 24 hours with aeration such that the superficial air velocity was 12.1. An assay of the nutrient medium following the fermentation revealed a yield of bacitracin amounting to 323 units/ml. This was more than twice the yields previously obtained. [Pg.126]

Early studies by Terawaki and Greenberg on the antibiotic activity of carzinophilin established that it inhibited DNA synthesis but not RNA or protein synthesis in E. coli strain Bo and in Bacillus subtilis [134]. They also found that exposure to carzinophilin removed the transforming capacity of B. subtilis DNA [135]. They... [Pg.415]

Bacterial amylase Bacillus subtilis Modified starch, sizing paper... [Pg.2]

Bacitracin Bacillus subtilis Gram-positive bacteria Wall synthesis... [Pg.268]

Antibiotic activities are examined by transfer of seed culture of Bacillus subtilis on nutrient agar on a Petri dish. The seed culture for Bacillus subtilis is a simple basal media of... [Pg.269]

Pseudomonas putida, Bacillus subtilis [l4C]Formate incorporates at C-2 of pyramine.78... [Pg.305]

In each cycle, the library of mutated genes is first inserted in a standard bacterial host such as Escherichia coli or Bacillus subtilis. Subsequently, bacterial colonies are plated out on agar plates and harvested individually by a colony picker. Each colony is placed in a separate well of a microtiter plate containing nutrient broth, so that the bacteria grow and produce the protein of interest. Because each colony originates... [Pg.21]

The Bacillus subtilis lipase A (BSLA) was the subject of two short directed evolution studies [19,47]. In one case systematic saturation mutagenesis at all of the ISlpositions of BSLA was performed [19]. Using meso-l,4-diacetoxy-2-cyclopentene as the substrate, reversed enantioselectivity of up to 83% ee was observed. In another study synthetic shuffling (Assembly of Designed Oligonucleotides) was tested using BSLA [47]. [Pg.38]

Hamasaki et al. (1992) reported that monobutyltin oxide, monobutyltin trichloride, and dibutyltin dichloride showed high SOS-inducing potency in the SOS chromotest with iiic/rerrc/rra co/r PQ 37. Dibutyltin dichloride and dimethyltin dichloride were also recognized as producing DNA damage by the rec-assay in Bacillus subtilis H 17 Rec and M45 Rec. Li et al. [Pg.31]

A comparison of the structures of penicillin and Dalanyl-Dalanine (cf. structures 41 and 42) shows that there is a great deal of similarity between the two molecules. Penicillin is essentially an acylated cyclic dipeptide of Dcysteine and Dvaline (84). As such, it contains a peptide bond, that of the /3-lactam ring, that can acylate the enzyme. Labeling studies of the peptidoglycan transpeptidase of Bacillus subtilis indicate that radioactive penicillin reacts with a sulfhydryl group of a cysteine residue of the enzyme (86). [Pg.403]

However, to date, no AMA studies have been conducted against spore-forming microorganisms. It is very important to search for a compound having action on the development of such organisms as Bacillus subtilis and B. cereus, since these microorganisms are able to withstand pasteurization conditions and contain hydrolytic enzymes, which generate off-flavor in the food. [Pg.17]

Fig. 4. a) Inhibition of microbial growth by GA, from Bacillus subtilis. Micrococcus luteus and Pseudomonas aeruginosa, b) Growth curve of Bacillus subtilis at 32 ° C ( ) Milk, (O) milk with addedGA47pM. [Pg.17]

In order to check whether the occurrence of the Rieske-type sequence motif is unique for the assimilatory nitrite reductase from Bacillus subtilis, the sequences of other assimilatory nitrite reductases were searched for the presence of the four putative ligands of Rieske-type clusters. A well-conserved sequence pattern... [Pg.92]


See other pages where Bacillus subtilis is mentioned: [Pg.84]    [Pg.141]    [Pg.250]    [Pg.300]    [Pg.285]    [Pg.406]    [Pg.406]    [Pg.406]    [Pg.409]    [Pg.33]    [Pg.78]    [Pg.94]    [Pg.155]    [Pg.296]    [Pg.412]    [Pg.127]    [Pg.126]    [Pg.126]    [Pg.1023]    [Pg.269]    [Pg.418]    [Pg.89]    [Pg.255]    [Pg.176]    [Pg.17]    [Pg.18]    [Pg.91]   
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Bacillus B. subtilis

Bacillus subtilis BPN

Bacillus subtilis Bacitracin

Bacillus subtilis a-amylase

Bacillus subtilis amino acid content

Bacillus subtilis amylase

Bacillus subtilis amyloliquefaciens

Bacillus subtilis antifungal activity against

Bacillus subtilis calcium

Bacillus subtilis characterization

Bacillus subtilis cloning

Bacillus subtilis cloning host

Bacillus subtilis cytochromes

Bacillus subtilis deoxyribonucleic acid

Bacillus subtilis effects of phenols

Bacillus subtilis enzyme activity

Bacillus subtilis enzymes

Bacillus subtilis expression

Bacillus subtilis extracellular

Bacillus subtilis extraction

Bacillus subtilis from spectra

Bacillus subtilis genome

Bacillus subtilis glucose metabolism

Bacillus subtilis induction

Bacillus subtilis intracellular

Bacillus subtilis lipase A

Bacillus subtilis lysis

Bacillus subtilis manganese transport

Bacillus subtilis neutral protease

Bacillus subtilis physiological role

Bacillus subtilis polymers

Bacillus subtilis properties

Bacillus subtilis protease

Bacillus subtilis protoplasts

Bacillus subtilis sensitivities

Bacillus subtilis sequence

Bacillus subtilis spore

Bacillus subtilis sporulation

Bacillus subtilis sporulation mutants

Bacillus subtilis strain

Bacillus subtilis substrate specificity

Bacillus subtilis subtilisin from

Bacillus subtilis synthesis

Bacillus subtilis transformation

Bacillus subtilis var. niger

Bacillus subtilis, electron

Bacillus subtilis, growth inhibition

Bacillus subtilis, growth inhibitory

Bacillus subtilis, inhibition

Bacillus subtilis, proteases from

Bacillus subtilis, proteolytic enzymes

Bacillus subtilis, subtilin

Bacterium Bacillus subtilis

Carbohydrase (Bacillus subtilis containing

Chorismate bacillus subtilis

Chorismate mutase from Bacillus subtilis

Effects on Bacillus subtili

Engineering of Genetic Traits in Bacillus subtilis

Hypericum brasiliense against Bacillus subtilis

Hypericum mysorense against Bacillus subtilis

INDEX Bacillus subtilis

Inhibition of Bacillus subtilis

Inhibitory activity Bacillus subtilis

Itoic acid Bacillus subtilis

Levansucrase from Bacillus subtilis

Metabolic engineering Bacillus subtilis

Microorganisms Bacillus subtilis

Minimal inhibitory concentration (MIC of Bacillus subtilis

Neutral protease from Bacillus subtili

Of Bacillus subtilis

Proteases of Bacillus subtilis

Pyrazines Bacillus subtilis

Starch hydrolysis Bacillus subtilis

Teichoic acids from Bacillus subtilis

The three-dimensional structure of Bacillus subtilis ferrochelatase

Vector Bacillus subtilis

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