Bacillus amyloliquefaciens amylase

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

Palva, I. (1982) Molecular cloning of alpha-amylase gene from Bacillus amyloliquefaciens and its expression in B. subtilis. Gene, 19 (1), 81-87. 

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... 

The organism that elaborates this a-amylase was originally called Bacillus subtilis. It was reclassified as Bacillus amyloliquefaciens in 1967.8... 

Figure 7.21 Determination of the structure of Bacillus amyloliquefaciens a-amylase limit dextrin, using enzymes no reaction with (3-amylase (b) reaction with pullulanase to give maltose + maltotriose (c) reaction of glucoamylase to give two tetrasaccharides, both ofwhich are eventually converted into panose + glucose. Analysis of the reactions can be made by thin layer chromatography239.

In the brewing industry, there is a development toward substitution of malt with unmalted barley and amylase, by use of glu-canase and protease of microbial origin. The neutral protease from Bacillus amyloliquefaciens and the thermostable neutral protease Bacillus subtilis var. thermoproteolyticus have been used by brewers successfully to hydrolyze barley proteins into amino acids and peptides. 

Carbohydrase and Protease, Mixed (Bacillus subtilis var. including Bacillus amyloliquefaciens) Produced as an off white to tan, amorphous powder or as a liquid by controlled fermentation using Bacillus subtilis 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, (2) /3-glucanase, (3) protease, and (4) pentosanase. Typical applications used in the preparation of starch syrups, alcohol, beer, dextrose, bakery products, and fishmeal in the tenderizing of meat and in the preparation of protein hydrolysates. 

Scanning electron micrograph of potato starch granule treated with Bacillus amyloliquefaciens ce-amylase, showing growth rings of the crystalline -amylase resistant starch in the granule... 

Dextran cyclic imidocarbonate has been used to prepare soluble conjugates of a-amylase from Bacillus amyloliquefaciens and of bovine liver catalase for use in experimental enzyme therapy. The results suggest that by coupling the enzymes with a poorly antigenic macromolecule (dextran) anaphylactic reaction in animals pre-immunized with dextran may be suppressed or eliminated. Trypsin has been immobilized by reaction with dextran cyclic imidocarbonate. 

Steyn, A. J. C., Pretoiius, I. S. (1991). Co-expression of a Saccharomyces diastaticus glucoatnylase-encoding gene and a Bacillus amyloliquefaciens alpha-amylase encoding gene in Saccharomyces cerevisiae. Gene, 100, 85-93. 

When growing under appropriate conditions, Bacillus amyloliquefaciens synthesizes a polysaccharide hydrolase (isoamylase) that selectively cleaves D-glucosidic linkages in branched a-o-glucans. " This enzyme appears to assist a-amylase in depolymerizing branched a-D-glucans. 

A depolymerization computer model, which uses a minimization routine to establish a subsite map for a depolymerase, has been applied to the experimental data for two a-amylases. An eight-subsite map was arrived at from the Km values and bond-cleavage frequencies for oligosaccharide substrates for Aspergillus oryzae a-amylase. Similarly ten subsites have been identified for Bacillus amyloliquefaciens a-amylase. 

The a-amylases from five strains of Bacillus amyloliquefaciens have been compared to determine whether differences in primary structure are responsible for variations in catalytic properties among the enzymes. Amino-acid analysis established virtually identical compositions for the proteins reaction with... 

Modificatimi of Enzymes and Uses of Modified En rmes a-Amylase.—Bacillus amyloliquefaciens a-amylase has been modified by covalent coupling with soluble dextran cyclic imidocarbonate and the stability of the resulting complex investigated. ... 

Lee, S., Y. Mouri, M. Minoda, H. Oneda, and K. Inouye. 2006. Comparison of the Wild-Type alpha-Amylase and Its Variant Enzymes in Bacillus Amyloliquefaciens in Activity and Thermal Stability, and Insights into Engineering the Thermal Stability of Bacillus alpha-Amylase. Journal of Biochemistry 139 (6) 1007-1015. 

The immunological properties of a-amylases from transformable, transformant, and DNA-donor strains of Bacillus amyloliquefaciens B. natto, and B. subtilis have been compared. Most of the enzymes cross-reacted with each other s antibodies and contain at least twelve common peptide sequences. However, distinct structural differences were noted e.g. only two of the enzymes contain carbohydrate, which consists of neutral sugars and 2-amino-2-deoxy-D-glucose (9—11% total). 

Dairy products and beverages are processed under mildly acidic conditions favoring the use of enzymes of fungal origin. However, in the processing of beer, the enzymes from selected Bacillus strains play an essential role. The a-amylase from Bacillus amyloliquefaciens is used to improve the enzymatic liquefaction potential of the malt. A P-glucanase from the same bacterium (Hofemeister et al. 1986) is used to reduce the viscosity of the wort, which improves the filtration of the beer. 

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