Bacillus subtilis amyloliquefaciens

P. Mantsala and M. Puntala, Comparison of levansucrase from Bacillus subtilis and from Bacillus amyloliquefaciens, FEMS Microbiol. Lett., 13 (1982) 395-399. 

Known producers of CGTase include Bacillus mascerans (7), Bacillus megaterium (8), Bacillus ohbensis (9), alkalophilic Bacillus sp. (lO M), Bacillus amyloliquefacien (15), Bacillus subtilis (16), Klebsiella oxytoca (17), and Micrococcus sp. (18), However, none of these CGTase enzymes are sufficiently thermostable for use in industrial starch liquefaction. 

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

Bacteria Bacillus subtilis Bacillus licheniformis Bacillus amyloliquefaciens... 

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. 

Carbohydrase and Protease, Mixed (Bacillus licheniformis var.), 20 Carbohydrase and Protease, Mixed (Bacillus subtilis var. including Bacillus amyloliquefaciens), 20 [2-Carboxy-P-(A-(h-methoxycarbonyl-2-phenyl)ethylcarbamoyl)]ethanaminium 6-Methyl-4-oxo-l,2,3-oxathiazin-3-ide-2,2-dioxide, 5... 

Bacillus subtilis var. including Bacillus amyloliquefaciens), 131, (S3)20 Carbohydrates (Starches, Sugars, and Related Substances), 836 Carbon, Activated, 85, (S 1)115 Carbonate Identification Test, 753 Carbon Dioxide, 87, (S 1)12 Carbon Dioxide Detector Tube, 862 Carbon Monoxide Detector Tube, 862 o-Carboxybenzeneazodimethylaniline Hydrochloride, 861 (R)-3-Carboxy-2-hydroxy-/V,/V,/V-... 

Carbohydrase and Protease, Mixed (Bacillus subtilis var. including Bacillus amyloliquefaciens), 131, 787, (S3)20... 

Deoxynojirimycin (DNJ) (14) Streptomyces lavandulae subsp. trehalostaticus no. 2882 [21] Bacillus amyloliquefaciens, Bacillus polymyxa. Bacillus subtilis [22] Moms sp. (Moraceae) roots [10,23] Moms bombycis (Moraceae) leaves [9]... 

Trichoderma reesei Bacillus subtilis Bacillus subtilis Bacillus amyloliquefaciens Trichoderma reesei Bacillus amyloliquefaciens Trichoderma reesei Bacillus amyloliquefaciens Serratia marcescens Escherichia coli Escherichia coli Nicotiana tabacum... 

Many kinds of microorganisms produce a-amylases. The enzymes are extracellular and are secreted into the environment of the organism for hydrolysis of starch. One of the early microbial a-amylases to be studied in some detail was Bacillus amyloliquefaciens a-amylase (formerly known as Bacillus subtilis liquefying a-... 

Peng, Y, Yang, X. J., Xiao, L., Zhang, Y. Z. Cloning and expression of a fibrinolytic enzyme (subtilisin DFE) gene from Bacillus amyloliquefaciens DC in Bacillus subtilis. Res Microbiol 2004,155, 167-173. 

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

Enzymes are highly specific catalysts. The nature of this specificity is believed to result from structural and electrostatic complementarity between the enzyme and its substrate. The serine protease, subtilisin, is being extensively studied as a model system to explore the effects of single amino acid substitutions on its structure and function Q). The gene for Bacillus amyloliquefaciens subtilisin has been expressed and secreted in B. subtilis 12).A site-directed mutagenesis scheme, cassette mutagenesis ( ), has been used to produce a series of subtilisin variants that are more resistant to oxidants (4), and have altered stability ( ), specificity, and specific activity. 

Many of today s industrial enzymes are produced hy Bacillus species, especially B. subtilis, B. amyloliquefaciens, and B. licheniformis. These include amylases. 

Curie-point pyrolysis MS was applied to the identification of selected Bacillus species by Shute et al. Fifty-three strains of B. subtilis, B. pumilus, B. licheniformis, and B. amyloliquefaciens in both a spomlating and nonspomlating state were pyro-... 

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). 

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