Showing papers on "Bacillus licheniformis published in 1976"

Membrane penicillinase of Bacillus licheniformis 749/C:sequence and possible repeated tetrapeptide structure of the phospholipopeptide region.

Abstract: The membrane penicillinase (EC 3.5.2.6; penicillin amido-beta-lactamhydrolase) of Bacillus licheniforis 749/C, which appears to be an intermediate in the formation of the exoenzyme, is a phospholipoprotein that carries an NH2-terminal chain of 24 amino acids (only serine, glycine, aspartic acid, asparagine, glutamic acid, and glutamine) and a phosphatidylserine that is not present in the exoenzyme.

Phosphatidylglycerol biosynthesis in Bacillus licheniformis Resolution of membrane-bound enzymes by affinity chromatography on cytidinediphospho-sn-1,2-diacylglycerol Sepharose.

Abstract: Cytidinediphospho-sn-1,2-diaclglycerol (CDP-diglyceride) has been covalently linked to Sephrose 4B via adipic acid dihydrazide spacer arm forming an effective affinity chromatography column. This liponucleo-tide ligand and sn-glycero-3-phosphate are subtracts for the formation of 3-sn-phoshatidyl-1'-sn-glycero-3'-phosphate (PGP) catalyzed in both eukaryotic and prokaryotic organisms by sn-glycero-3-phosphate: CMP phosphatidlytranferase (PGP synthetase). Using this CDP-diglyceride Sephrose affinity column we were able to resolve the membrane associated 3-sn-phosphatidyl'1-sn-glycerol (PG) synthesizing system present in Bacillus licheniformis into two activities. A PGP synthetase activity was adsorbed to the affinity column and was eluted using buffer containg CDP-diglyceride; a PGP phosphatease acactivity had no affinity for the column. Both PGP synthase and PGP phosphatase of B. licheniformis were associated with a membrane component of the cell as evidenced by sucrose gradient centrifugation, differential centrifugation, and solubilization by buffers containing detergent...

Numerical Taxonomy of Bacillus Isolates from North Sea Sediments

Abstract: A numerical taxonomic study of 138 Bacillus strains isolated from North Sea sediments is presented The clustering process, based on 63 selected multistate features, resulted in the formation of two clusters separated by the Voges-Proskauer reaction Further subdivision yielded six phenons, one of which corresponded to the conventional species Bacillus licheniformis The strains, taken in the order in which they appeared in the dendrogram, exhibited a gradient in the frequency of positive answers to biochemical and physiological tests

Teichoic acids and lipids associated with the membrane of a Bacillus licheniformis mutant and the membrane lipids of the parental strain.

Abstract: Bacillus licheniformis 6346 MH-1 and a phosphoglucomutase-deficient poorly lytic mutant, B. licheniformis 6346 MH-5, both contain cardiolipin, phosphatidyl ethanolamine, and phosphatidyl glycerol but are devoid of phosphoglycolipids. Gentiobiosyl diglyceride is present in the parent organism but glycolipids are absent from the mutant. Lipoteichoic acid was extracted from the whole cells of MH-5 with hot aqueous phenol and contained fatty acids, glucosamine, and 1,3-polyglycerol phosphate. The fatty acids were predominantly of the branched-chain type and were esterified to hydroxyl groups of a terminal glycerol residue. The polyglycerol phosphate chains contained, on average, 32 to 40 glycerol residues, some of which were substituted at the secondary hydroxyl group with alpha-N-acylglucosaminyl residues. Phenol extraction of the supernatant fluid that remained when walls were removed from preparations of disrupted cells of MH-5 yielded membrane teichoic acid, which consisted of substituted polyglycerol phosphate but was devoid of fatty acids.

On the Role of Bacitracin Peptides in Trace Metal Transport by Bacillus licheniformis

Abstract: SUMMARY: Bacitracin markedly increased the toxic effect of several divalent metal ions towards growth of the producer strain Bacillus licheniformis ATCC14580. Magnesium ions antagonized the toxic effect of these divalent cations both in the presence and absence of bacitracin. It is suggested that bacitracin increases the uptake of several divalent metal ions. The function of the bacitracin peptides may be to extract essential divalent cations from ‘waiting sites’ on the surface of the cells and transfer the cations to the transport mechanisms in the cytoplasmic membrane.

Inhibition of Clostridium perfringens by an Antibiotic Substance Produced by Bacillus licheniformis in the Digestive Tract of Gnotobiotic Mice: Effect on Other Bacteria from the Digestive Tract

Abstract: A strain of Bacillus licheniformis, established in the digestive tract of gnotobiotic mice, inhibited the subsequent establishment of a Clostridium perfringens strain ingested by the animals. This inhibitory effect depended on the in vivo production by B. licheniformis of an antibiotic substance having a number of the characteristics of bacitracin. If C. perfringens was the first to become established in the digestive tract of the gnotobiotic mice, B. licheniformis also became established but did not produce any antibiotic. Mutants of C. perfringens resistant to the antibiotic substance were not observed when the antibiotic was produced in situ by B. licheniformis, but were rapidly selected when the Bacillus culture filtrate or bacitracin was administered per os. B. licheniformis was also capable of eliminating from the digestive tract 5 of the 13 additional bacterial strains tested.

Lipoteichoic acid from Bacillus licheniformis 6346 MH-1. Comparative studies on the lipid portion of the lipoteichoic acid and the membrane glycolipid.

Abstract: A lipoteichoic acid and a membrane glycolipid were isolated from Bacillus licheniformis 6346 MH-1. The fatty acid composition of the two preparations were similar. Most of the fatty acids were of the branched chain type. The glycolipid was shown to be a diacyl derivative of O-beta-D-glucopyranosyl-(1 leads to 6)-O-beta-D-glucopyranosyl-(1 leads to 3)-glycerol. The lipoteichoic acid contained lipid, polyglycerol phosphate, and glucosamine. The lipid was released by treatment with hydrofluoric acid and by hydrolysis in dilute acid and was shown to have a structure identical with that of the membrane glycolipid.

Subunits of the alkaline phosphatase of Bacillus licheniformis: chemical, physicochemical, and dissociation studies.

Abstract: The alkaline phosphatase (orthophosphoric monoester phosphydrolase, EC 3.1.3.1) of Bacillus licheniformis MC14 was studied in an attempt to determine the number of subunits contained in the 120,000-molecular-weight native enzyme. Two moles of arginine was liberated per mole of native enzyme by carboxypeptidases A and B in the presence of sodium dodecyl sulfate. The effect on the native enzyme of progressively lowering the solvent buffer pH was monitored by determining the molecular weight by sedimentation equilibrium analysis, the sedimentation coefficient, the frictional coefficient, and the percent alpha-helix content of the enzyme. The alkaline phosphatase dissociates into two subunits around pH 4. At pH 2.8 a further decrease in S value, but no change in molecular weight, is observed, indicating a change in conformation. The frictional coefficients and percent alpha-helix content agree with this interpretation. A subunit molecular weight of 59,000 was calculated from sodium dodecyl sulfate gels. Images

Light-induced inhibition of sporulation in Bacillus licheniformis.

Abstract: Sporulation of Bacillus licheniformis is inhibited by broad-spectrum light. This phenomenon is intensity dependent and is a near-ultraviolet and blue light effect.

Occurrence in Bacillus licheniformis of Two Species of 5‐S RNA with Multiple Differences in Primary Structure

Abstract: Bacillus licheniformis was found to contain two species of 5-S RNA. One of these, the primary structure of which has been published previously [H. A. Raue, T. J. Stoof and R. J. Planta (1975) Eur. J. Biochem. 59, 35–42] accounts for 80–90% of the total cellular amount of 5-S RNA. The other one, comprising 1–20% of the total amount, differs in primary structure from the major species at eight positions. All base changes are either purinepurine or pyrimidinepyrimidine substitutions. Half of the changes are located within the 5′-termiiial part (15 nucleotides) of the molecule, the other half in the 3′-terminal region (22 nucleotides). At least one of the base changes is in a region which in B. subtilis has been implicated in processing of precursor 5-S RNA. The data are consistent with the existence of a single 5-S RNA cistron with a primary structure different from-that of all other 5-S RNA cistrons in B. licheniformis.

Protease inactivated α-amylase preparations

Abstract: Protease enzyme impurities contained in bacterial α-amylase enzyme preparations are inactivated by a mild heat treatment in the presence of a protective material. Useful protective materials include calcium and starch hydrolysates such as corn syrup. The protease-free α-amylase can then be used to solubilize starch materials by various granular starch and conventional processes. Hydrolysates obtained contain significantly less soluble protein than those prepared using untreated α-amylases. A preferred α-amylase enzyme preparation is one derived from a Bacillus licheniformis microorganism.

Process for preparing glucoamylase

Abstract: Glucoamylase is prepared by fermenting a microorganism capable of producing glucoamylase in a nutrient medium containing at least about 16% to about 25% of ground corn which has been liquefied by the action of heat, water and an alpha-amylase enzyme preparation. The alpha-amylase enzyme preparation is preferably derived from a microorganism of Bacillus licheniformis.