Bacillus subtilis calcium

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. 

Toda, T. et al.. New 6-0-acyl isoflavone glycosides from soybeans fermented with Bacillus subtilis (natto). I. 6-0-succinylated isoflavone glycosides and their preventive effects on bone loss in ovariectomized rats fed a calcium-deficient diet, Biological Pharmaceutical Bulletin, 22, 1193, 1999. 

The physiological role of PHB/polyP complexes has not been established, but bacterial cells like eukaryotic cells maintain low internal Ca2+,101-103,112 and there is increasing evidence pointing to calcium involvement in a number of important cellular functions, such as chemotaxis, cell division, heat shock, pathogenicity, and differentiation.104-107 Systems for calcium export have been identified.108-109 Mechanisms for calcium entry are less well known. An L-type channel was reported in Bacillus subtilis,n0 lu and Jones et al. and Holland et al.103,112 recently demonstrated the presence of a putative Ca2+ influx channel in stationary phase E. coli,... 

The various a-amylases contain, per mole, at least one gram-atom of firmly bound calcium, which is required both for enzymic activity and to prevent destruction of the amylases by proteolytic enzymes. Bacillus subtilis a-amylase is unusual in that it also contains small proportions of zinc and exists as a dimer which is crosslinked by a zinc atom. Removal of the zinc does not inactivate the enzyme. 

Fe (2 ppm), casein hydrolyzate (0.2 g/dl), yeast extract (0.2 g/dl), corn steep liquor (0.2 ml/dl), polypeptone (0.1 g/dl), meat extract (0.1 g/dl) and sodium ribonucleate (10 mg/dl) were poured into respective test tubes and each tube was sterilized at 115°C for 10 minutes. Thereafter separately sterilized calcium carbonate was added in the amount of 2 g/dl and then cells of Bacillus subtilis S26910 were inoculated into the above media and cultured with shaking at 30°C for 20 hours. 

Similarly, chemotactic behaviour of bacteria is controlled by Ca . Mobile bacteria swim towards certain chemicals and away from others. Such bacteria can swim smoothly in a straight line or tumble, which results in random changes in direction. When heading towards repellents bacteria tumble more frequently to increase the probability of swimming away. Influx of Ca causes tumbling. Such behaviour has been found for Bacillus subtilis but apparently not for E. co/i. Calcium accelerates the swimming speed of Chlamydomonas reinhardii and regulates reverse motion in phototactically active Phormidium uncinatum and Halobacterium halobium. Phototaxis in H. halobium involves a methylation-demethylation process which is calcium dependent. Attractant stimuli raise the level of methylation of membrane proteins, while repellent stimuli cause demethylation and the enhanced opportunity for reversal of direction. Ca " " deactivates the methyl transferase and activates a methyl esterase. ... 

Bacillus cereus calcium transport, 572 Bacillus megaterium calcium efflux, 570 calcium transport, 572 sporulation zinc transport, 572 Bacillus spp. sodium ions, 559 sporulation calcium transport, 571 BacUlus subtilis manganese transport, 570 sporulation... 

Toma, S., Campagnoli, S., Maigarit, I., Gianna, R., Grandi, G., Bolognesi, M., Filippis, i.D., Fontana, A. 1991, Grafting of a calcium-binding loop of thermolysin to Bacillus Subtilis neutral protease. 

O -Amylase K is a novel thermostable a-amylase from Bacillus subtilis which produces maltohexaose from starch.Various methods showed the existence of two forms which did not differ significantly in action and which may therefore be isoenzymes. a-Amylase K is stable at 60 in the presence of additional calcium chloride with 80% activity remaining after 6 days. It is completely deactivated after 10 min at 90 and inhibited by tris-(hydroxy-methyl)-aminomethane above pH 5.0. The purified a-amylase K fractions are less thermostable than the original enzyme solution. a-Amylase K is stable to freeze drying but reconstituted enzyme solution was less active at pH-values below 5.8. 

Fujisawa M, Wada Y, Tsuchiya T, Ito M. Characterization of Bacillus subtilis YfkE (ChaA) a calcium-specific Ca2+/H+ antiporter of the CaCA family. Arch Microbiol. 2009 191 649-57. 

Taka amylase a bacterial a-amylase (EC 3.2.1.1) isolated and crystallized from Aspergillus oryzae taka diastase preparations. T. a. (Af, 50,000) is a calcium-containing, single-chain protein with V-terminal alanine and C-terminal serine. Like the tetrameric Bacillus subtilis a-amylase (Af, 96,000), T.a. is resistant to sodium dodecylsulfate but is reversibly denatured by 6 M guanidine or 8 M urea. T.a. must not be confused with Adenosine deaminase (see), which is also present in taka diastase. 

It is industrially prepared by the fermentation of sugar or starch, brought about by the addition of putrefying cheese, with calcium carbonate added to neutralize the acids formed in the process. The butyric fermentation of starch is aided by the direct addition of Bacillus subtilis. Salts and esters of the acid are called butanoates. 

A condition in breads caused by Bacillus mesentericus or Bacillus subtilis. Spores of these bacteria can survive baking and then germinate under proper moisture and temperature surroundings. The bread develops sticky yellow patches that can be pulled into ropelike threads hence, the name rope. Obviously, the bread is inedible. Food additives such as calcium acetate, calcium propionate, and sodium diacetate retard this bacterial growth. 

Kuhla, B., D. Albrecht, S. Kuhla and C.C. Metges, 2009. Proteome analysis of fatty liver in feed deprived dairy cows reveals interaction of fuel sensing, calcium, fatty acid and glycogen metabolism. Physiol Genomics 37, 88-98. Eymann, C., D. Becher, J. Bernhardt, K. Gronau, A Klutzny and M. flecker, 2007. Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7, 3509-3526. 

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