Bacillus licheniformis

In 1958, the microbial alkaline protease Alcalase (Novo Industries) was produced by fermentation of a strain of Bacillus licheniformis. It had high StabiHty and activity at pH 8—10, was marketed in 1961, and was incorporated into Bio 40. However, it was not until the successful marketing of the presoaking agent Biotex in 1963 that detergent manufacturers saw the tme possibiHties of enzymes. 

A.mylases. Commercial laundry amylases comprise the a-amylase from bacillus amyloliquefaciens and the heat-stable a-amylase from bacillus licheniformis. 

In the alcohol industry, grain or potato raw materials are milled and water added to form a slurry or mash which is heated either batchwise or continuously. Traditionally, the mash is heated to 150°C by the injection of Uve steam. To reduce viscosity, a-amylases are added both during beating to 150°C and during cooling. Thermostable a-amylases from Bacillus licheniformis are the most commonly used enzymes for these processes (68). 

Fig. 15. En2ymatic hydrolysis of wheat gluten at 72.5°C and pH 7.5 by an alkaline protease from Bacillus licheniformis. The numbers on the curves are en2yme—substrate ratios (E/S) in activity units (AU)/kg of protein where S = 7.4% (N x 5.7).

Bacillus licheniformis produces a water-insoluble levan that has potential application as a selective plugging agent in MEOR. The microorganisms grow on sucrose, glucose, and fructose but produce levan only on sucrose. Thus plugging may be selectively controlled in the reservoir by substrate manipulation. Oil reservoirs that have a temperature of less than 55° C, a pH between 6 and 9, a pressure less than 500 atm, and a salt concentration of 4% or less are potentially suitable [1480]. 

S. C. Lin, J. C. Goursaud, P. J. Kramer, G. Georgiou, and M. M. Sharma. Production of biosurfactant by Bacillus licheniformis strain JF-2. In E. C. Donaldson, editor. Microbial enhancement of oil recovery recent advances Proceedings of the 1990 International Conference on Microbial Enhancement of Oil Recovery, volume 31 of Developments in Petroleum Science, pages 219-226. Elsevier Science Ltd, 1991. 

J. A. Ramsay, D. G. Cooper, and R. J. Neufeld. Effects of oil reservoir conditions on the production of water-insoluble levan by Bacillus licheniformis. GeomicrobiolJ, 7(3) 155-165, July 1989. 

Figure 11.3 Positive ion FIESMS spectra of crude cell extracts from Escherichia coli HB101 (A), Bacillus sphaericus DSM 28 (B), and Bacillus licheniformis NTCC 10341 (C). (D) A pseudo-3D plot of the first three discriminant functions (DF1-3) obtained from positive ion whole-cell DIESMS spectra of seven Bacillus subtilis strains (a-g) (E) the corresponding abridged dendrogram obtained from the same information as in D. (Adopted from Vaidyanathan et al.57)...

Thus the alkaline protease obtained from Bacillus licheniformis with a molecular mass of about 27 000 consists of 274 amino acid residues and has serine and histidine as active sites. Pancreatic trypsin with a molecular mass of about 24 000 contains 230 amino acid residues and also has serine and histidine as active sites. Papain (molecular mass about 23 000 and 211 amino acid residues) has cysteine and histidine as active sites. 

M. Faijes, X. Perez, O. Perez, and A. Planas, Glycosynthase activity of Bacillus licheniformis 1,3-1,4-beta-glucanase mutants Specificity, kinetics, and mechanism, Biochemistry, 42 (2003) 13304—13318. 

King EC, Watkins WJ, Blacker AJ et al (1998) Covalent modification in aqueous solution of poly-y-D-glutamic acid from Bacillus licheniformis. J Polvin Sci A Polym Chem 36 1995-1999... 

Prodhomme EJF, Tutt AL, Glennie MJ et al (2003) Multivalent conjugates of poly-y-D-glutamic acid from Bacillus licheniformis with antibody F(ab ) and glycopeptide ligands. Bioconjug Chem 14 1148-1155... 

Tinglu, G., Ghosh, A., and Ghosh, B.K. (1984) Subcellular localization of alkaline phosphatase in Bacillus licheniformis 749/C by immunoelectron microscopy with colloidal gold. J. Bacteriol. 159, 668. 

Daughney CJ, Fein JB (1998) The effect of ionic strength on the adsorption of H+, Cd2+, Pb2+, and Cu2+ by Bacillus subtilis and Bacillus licheniformis a surface complexation model. J Colloid Interface Sci 198 53-77... 

Phenylacetic acid has been detected in fermented soya bean made with the strain Bacillus licheniformis as a starter, but has not been present in extracts of nonfermented soya bean. The phenylacetic acid produced by Bacillus licheniformis during the fermentation of soya bean is one of the main compounds of antimicrobial activity of Chungkook-Jang, a traditional Korean fermented-soya bean food with antimicrobial properties (Kim and others 2004). 

Kim Y, Cho JY, Kuk JH, Moon JH, Cho JI, Kim YC and Park KH. 2004. Identification and antimicrobial activity of phenylacetic acid produced by Bacillus licheniformis isolated from fermented soybean, Chungkook-Jang. Curr Microbiol 48(4) 312—317. 

The effectiveness of bacteriocins is often a function of environmental factors such as pH, temperature, food composition, structure, and food microflora (De Vuyst and Leroy 2007). A novel bacteriocin-like substance produced by Bacillus licheniformis P40 inhibits the activity of the soft rot bacterium Envinia carotovora. This compound caused a bactericidal effect on the pathogen cells at a 30 p.g/mL concentration (Cladera-Olivera and others 2006). 

Enzymes Proteases Various bacilli, e.g. Bacillus licheniformis... 

Similar studies showed a positive association between HLA alleles and development of IgE antibody. Sensitized platinum workers were DR3+ and DR6- while non-sensitized workers were DR3- and DR6+ [37], The linkage between HLA phenotype and development of IgE antibody was greatest among the low exposure group. A second study showed a relationship between HLA DR3 and IgE to inhaled anhydrides [38], A study among detergent workers showed a positive association between HLA-DR4+ and IgE antibody to the serine protease derived from Bacillus licheniformis [39],... 

A practical enzymatic procedure using alcalase as biocatalyst has been developed for the synthesis of hydrophilic peptides.Alcalase is an industrial alkaline protease from Bacillus licheniformis produced by Novozymes that has been used as a detergent and for silk degumming. The major enzyme component of alcalase is the serine protease subtilisin Carlsberg, which is one of the fully characterized bacterial proteases. Alcalase has better stability and activity in polar organic solvents, such as alcohols, acetonitrile, dimethylformamide, etc., than other proteases. In addition, alcalase has wide specificity and both l- and o-amino acids that are accepted as nucleophiles at the p-1 subsite. Therefore, alcalase is a suitable biocatalyst to catalyse peptide bond formation in organic solvents under kinetic control without any racemization of the amino acids (Scheme 5.1). 

Novozymes, a subtilisin produced by Bacillus licheniformis, was used by Chen et al ° to carry out a dynamic kinetic resolution of benzyl, butyl, or propyl esters of DL-phenylalanine, tyrosine, and leucine. The hydrolysis was performed at pH 8.5 in 2-methyl-2-propanol/water (19 1) and the freed L-amino acids precipitated. The key feature bringing about continual racemization of the remaining D-amino acid esters was the inclusion of 20 mmol 1 pyridoxal phosphate. 

Thermostability of Thermoanaerohacter sp. CGTase. The addition of 40ppm Ca+ + to the CGTase preparation during incubation at high temperatures in the absence or presence of starch substrate provided no enhancement of the thermostability of the enzyme. A comparison of the thermostable CGTase was made to other thermostable enzymes used in starch liquefaction including Termamyl Bacillus licheniformis) and Bacillus stearothermophilus alpha-amylase. 

Supek V, Gamulin S, Delic V. (1985) Enhancement of bacitracin biosynthesis by branched-chain amino acids in a regulatory mutant of Bacillus licheniformis. Folia Microbiol 30 342-348. 

From Corynebacterium glutamicum the siderophore corynebactin was obtained (47). It differs from enterobactin in being composed of three DHB-Gly-L-Thr units (Fig. 7, 24). Later the same siderophore was fotmd to be produced also by Bacillus subtilis and named bacillibactin (223). Its complexation constant is (S4). The monomeric unit DHB-Gly-Thr was isolated from Bacillus licheniformis (357a). 

Lipase, which is highly useful for kinetic resolution, however, has a limitation for use in DKR in that it carmot be used for (S)-configuration products. For this purpose, subtiHsin, a protease from Bacillus licheniformis, can replace lipase since it provides complementary enantioselectivity (Scheme 1.4). Subtilisin, however, has been much less frequently employed in resolution compared to lipase because it displays poor catalytic performance in organic media. Subtilisin is inferior to lipase in several properties such as activity, enantioselectivity and stability. Accordingly, the use of the enzyme usually requires some special treatments for activation and stabilization before use. For example, the treatment of subtilisin with surfactants has enhanced substantially its activity and stability up to a synthetically useful level. 

Enz5mies Proteases Amylases Cellulases Various Bacilli, e.g. Bacillus licheniformis Bacillus subtilis, Aspergillus oryzae Trichoderma viride, Penicillium pinophilum... 

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