Bacillus licheniformis amylase

Declerck N, Machius M, Wiegand G, Huber R, Gaillardin C (2000), Probing structural determinants specifying high thermostability in Bacillus licheniformis-amylase ,/ Mol. BioZ.,301,1041-1057. 

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). 

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. 

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

American-Maize Products Co., Hammond, IN), ordinary corn (Maltrin M-250, Grain Processing Corp., Muscatine, lA) and potato (Avebe America Inc., Hopelawn, NJ) hydrolysates were obtained commercially. Wheat, cassava, rice, and amylomaize VII starches were enzymatically hydrolyzed using a thermally stable alpha-amylase from Bacillus licheniformis (E.C.3.2.1.1 ... 

Disulfide interchange was also found to dominate mostly in another case the difference in half-lives r1/2 at 90°C and pH 6.5 of Bacillus a-amylases extended two orders of magnitude from Bacillus amyloliquefaciens through B. slearolhermophilus to B. licheniformis (Tomazic, 1988). For B. licheniformis a-amylase, deamidation of Asn/Gln residues was the main cause of inactivation. The cause of thermostability... 

Carbohydrase and Protease, Mixed (Bacillus licheniformis var.) Produced as an off white to brown, amorphous powder or as a liquid by controlled fermentation using Bacillus licheniformis var. Soluble in water (the solution is usually light yellow to dark brown), but practically insoluble in alcohol, in chloroform, and in ether. Major active principles (1) a-amylase and (2) protease. Typical applications used in the preparation of starch syrups, alcohol, beer, dextrose, fishmeal, and protein hydrolysates. 

Application and Principle This procedure is used to determine the a-amylase activity, expressed as bacterial amylase units (BAU), of enzyme preparations derived from Bacillus subtilis var., Bacillus licheniformis var., and Bacillus stearoth-ermophilus. It is not applicable to products that contain 13-amylase. The assay is based on the time required to obtain a standard degree of hydrolysis of a starch solution at 30° 0.1°. The degree of hydrolysis is determined by comparing the iodine color of the hydrolysate with that of a standard. 

The melting and crystallization behaviors observed for PCL and PLLA enzymatically coalesced with the alpha-amylase enzyme from Bacillus licheniformis, indicate that they might lead to superior drug carriers when coalesced from common CD-ICs also containing drugs (see Fig. 13). The rapid solidification of PCL... 

Typically, the amylases used in detergent are derived from bacterial sources. B. licheniformis amylase is particularly desirable for detergent applications as it is highly thermostable and maintains its activity even at high pH. The primary drawback of Bacillus-derived amylases as detergent enzymes is that their stability (and in many cases also their activity) relies on bound Ca. ions.f This is problematic in detergent formulations that must also contain detergent builders to limit water hardness. Oxidation of a methionine residue close to the active site of B. licheniformis amylase is another common stability problem. ... 

During liquefaction, the starch is solubilized by heating and partially hydrolyzed with a thermostable alpha amylase from Bacillus licheniformis or from other sources. The endo-acting alpha amylases are able to bypass the a-(l->6)-D-glucosidic linkages at the branch points in amylopectin but are not capable of hydrolyzing them. The oligosaccharides formed can be branched or linear. The... 

E1 = a -amylase, enzyme from Bacillus licheniformis E2 = glucoamylase, enzyme from Aspergillus niger... 

Figure 7 A hypothetical pathway by which an all beta sheet protein (a) might evolve into an all alpha-helical protein (h) by a series of insertions and deletions. Beta sheets are designated by lower case letters and alpha helices by upper case letters. Red arrows indicate a clear evolutionary relationship, orange arrows indicate a possible evolutionary relationship, and black arrows indicate no evolutionary relationship, (a) C-terminal domain of Bacillus licheniformis a-amylase (1BPL) ...

Declerck N, Machius M, Joyet P et al. (2003) HyperthermostabUization of Bacillus licheniformis ot-amylase and modulation of its stability over a 50°C temperature range Prot Eng 16(4) 287-293... 

Enzyme production kinetics in SSF have the potential to be quite complex, with complex patterns of induction and repression resulting from the multisubstrate environment. As a result, no mechanistic model of enzyme production in SSF has yet been proposed. Ramesh et al. [120] modeled the production of a-amylase and neutral protease by Bacillus licheniformis in an SSF system. They showed that production profiles of the two enzymes could be described by the logistic equation. However, although they claimed to derive the logistic equation from first principles, the derivation was based on a questionable initial assumption about the form of the equation describing product formation kinetics They did not justify why the rate of enzyme production should be independent of biomass concentration but directly proportional to the multiple of the enzyme concentration and the substrate concentration. As a result their equation must be considered as simply empirical. 

Declerek, N., Machius, M., Joyet, R, Wiegand, G., Huber, R., and Gaillardin, C. (2003). Hyper thermostabilisation of Bacillus licheniformis a amylase and modulation of its stability over a 50 C temperature range,... 

Amylase Aspergillus oryzae, Aspergillus niger, Rhizopus sp., Bacillus amyloliquifaciens, Bacillus licheniformis, Bacillus coagulans... 

Ul-Haq, L, H. Ashraf, and S. Ali. 2007. Kinetic Characterization of Extracellular Alpha-Amylase from a Derepressed Mutant of Bacillus Licheniformis. Applied Biochemistry and Biotechnology 1 (3) 251-164. 

Table 1. Effect of Carbon Sources on the Synthesis of a-amylase by Bacillus licheniformis and Streptomyces limosus...

Fig. 2 Growth, 0, a-amylase synthesis, , and glucose consumption for Bacillus licheniformis NCIB 6346 (closed symbols) and the catabolite dere-pressed mutant RMIO (open symbols) Medium was minimal salts (Thiruna-vukkarascu and Priest, 1984) containing glucose (0.2%) and yeast extract (0.05%).

Fig. 2.49. The activity of a-amylase as influenced by temperature. 1 a-amylase from Bacillus subtilis, 2 from Bacillus licheniformis...

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