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Bacillus stearothermophilus amylase

Application and Principle This procedure is used to determine maltogenic amylase activity in preparations derived from Bacillus subtilis containing a Bacillus stearothermophilus amylase gene. The test is based on a 30-min hydrolysis of malto-triose under controlled conditions and measurement of the glucose formed by high-performance liquid chromatography (HPLC). [Pg.916]

Enzymes. Termamyl, AMG, and Dextrozyme were obtained from Novo Nordisk Bioindustrials, Inc., Danbury, CT. Bacillus stearothermophilus alpha-amylase was supplied by Enzyme Bio-Systems Ltd., Englewood Cliffs, NJ. [Pg.385]

Liquefaction - Lab-Scale. 35% DS com starch slurries were liquefied with the CGTase at a dose of 4.46 Phadebas units/gram DS starch at pHs 4.5-5.5 for 14 minutes at 105 C (primary liquefaction) and for 4 hours at 90 (secondary liquefaction) +/- 40 ppm calcium. Final volumes were 5-10 ml. Termamyl and Bacillus stearothermophilus alpha-amylase were run as controls at pHs 6.2 and 5.8, respectively in the presence of 40 ppm calcium. [Pg.386]

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. [Pg.387]

In the case of enzymes, the rate of the catalysed reaction increases regularly with increasing temperature. However, the probability of the unfolding of the threedimensional conformation of the protein molecule also increases, as there is more energy available to split the non-covalent interactions between side chains. In some cases it has been demonstrated that such noncovalent interactions play a dominant role in the stability of the native conformation. For example, Brosnan, Kelly and Fogarty (1992) demonstrated that the irreversible thermoinactivation of -amylase of Bacillus stearothermophilus at 90°C is related to changes of the hydrophobic interactions in the molecule. [Pg.320]

Carbohydrase (Bacillus stearothermophilus) Produced as an off white to tan powder or a light yellow to dark brown liquid by controlled fermentation using Bacillus stearothermophilus. Soluble in water, but practically insoluble in alcohol, in ether, and in chloroform. Major active principle a-amylase. Typical applications used in the preparation of starch syrups, alcohol, beer, dextrose, and bakery products. [Pg.148]

Carbohydrase (Bacillus acidopullulyticus), 19 Carbohydrase (Bacillus stearothermophilus), 19 Carbohydrase (Bacillus subtilis containing a Bacillus megaterium CL-amylase gene), 19 Carbohydrase (Bacillus subtilis containing a Bacillus... [Pg.112]

L Holm, A Koivula, P Lehtovaara, A Hemminki, J Knowles. Random mutagenesis used to probe the structure and function of Bacillus stearothermophilus alpha-amylase. Protein Eng 3 181-191, 1990. [Pg.321]

The synthesis of amylase in Ps. saccharophila (40) and Bacillus stearothermophilus (24) is stimulated by degradation products of starch as much as or much more than starch itself. But, such relationships could... [Pg.72]

Obeig CJ, Merrill RK, Brown RJ et al. (1992) Effects of milk-clotting enzymes on physical properties of mozzarella cheese. J Dairy Sd 75 669-675 Ogasahara KJ, Imanishi A, Isemura T (1970) Studies on thermophilic a-amylase from Bacillus stearothermophilus II. Thermal stability of thermophihe a-amylase. J Biochem 67(l) 77-82 Ogawa J, Shimizu S (1999) Microbial enzymes new industrial applications from traditional screening methods. TIBTECH 17 13-21... [Pg.100]

Scheirlinck et al. (1989), have successfully introduced amylase- and endogluconase-encoding plasmids from Bacillus stearothermophilus to Lactobacillus plantarum by electrophoration. [Pg.20]

For starch to be effectively degraded it must first be heated above 65 °C. The starch grains then burst and they form a viscous gel. This must be thinned so that the viscosity is low enough for the dispersed starch to be handled. The a-amylase from barley is fairly stable to heat, and it is active at 65 °C. However some a-amylases from the organisms which grow at temperatures up to 80° or 90 °C (e.g. Bacillus stearothermophilus) are stable for short periods at temperatures above 100°C, and these heat-stable enzymes are very useful for the controlled thinning of starch gels. [Pg.334]

Production of a-amylase by Bacillus stearothermophilus (pAT9) and Gene Manipulation to Improve the Stability of the Recombinant Plasmid... [Pg.1]

PRODUCTION OF a-AMYLASE BY BACILLUS STEAROTHERMOPHILUS (pAT9) AND GENE MANIPULATION TO IMPROVE THE STABILITY OF THE RECOMBINANT PLASMID... [Pg.113]

THERMOSTABLE ALPHA AMYLASE OF BACILLUS STEAROTHERMOPHILUS CLONING, EXPRESSION, AND SECRETION BY ESCHERICHIA COLI... [Pg.129]

Manning, G. B., and Campbell, L. L., 1961, Thermostable Alpha-Amylase of Bacillus Stearothermophilus, J. Biol. Chem., 236 2952. [Pg.146]

CocconceUi PS, Gasson MJ, Morelli L, Bottazzi V (1991) Single-stranded DNA plasmid vector construction and cloning of Bacillus stearothermophilus a-amylase in Lactobacillus. Res Microbial 142 643-652 Crow VL (1987) Citrate cycle intermediates in the metabolism of aspartate and lactate by Propionibacterium freudenreichii subsp. shermanii. Appl Environ Microbiol 53 2600-2602... [Pg.69]

Aiba Sy Kitai Imanaka T (1983) Cloning and expression of thermostable alpha-amylase gene from Bacillus stearothermophilus in Bacillus stearothermophilus and Bacillus subtilis. Appl Environ Microbiol 46 1059-1065... [Pg.207]

Gray GL, Mainzer SE, Rey MW, Lamsa MH, Kindle KL, Carmona C, Requadt C (1986) Structural genes encoding the thermophilic alpha-amylases of Bacillus stearothermophilus and Bacillus licheniformis. J Bacteriol 166 635-643... [Pg.208]

Amylases classified in family 13 glycoside hydrolases have been described from the archaea to the bacteria domains. The genus Bacillus includes a set of species able to produce starch-d rading enzymes and has biotechnological potential as a source of these enzymes especially the a-amylases, which are the most fi equent starch-degrading enzymes described for bacteria. In addition. Bacillus a-amylases present activity and are stable in temperatures over 50-60 °C, therefore are very attractive for industrial applications. B. subtilis, Bacillus stearothermophilus. Bacillus lichenifortnis, and Bacillus atnyloliquefaciens have been widely used for commercial production of amylases and for the production of starch derivates. The a-amylases produced by other bacteria and also archaea have to compete with the Bacillus enzymes that already present excellent thermophilic properties and high conversion rates (Prakash and Jaiswal 2010). [Pg.219]

Nonato, R. V, Shishido, K. a-factor-directed synthesis of Bacillus stearothermophilus a-amylase mSaccharomyces cerevisiae. BiochemBiophysRes Com. 2000,152, 76-82. [Pg.276]

See other pages where Bacillus stearothermophilus amylase is mentioned: [Pg.335]    [Pg.896]    [Pg.111]    [Pg.120]    [Pg.400]    [Pg.73]    [Pg.691]    [Pg.100]    [Pg.207]    [Pg.38]    [Pg.1]    [Pg.125]    [Pg.129]    [Pg.81]    [Pg.30]    [Pg.30]    [Pg.197]    [Pg.206]    [Pg.1196]    [Pg.368]    [Pg.129]   


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Bacillus stearothermophilus

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