Bacillus amyloliquefaciens

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

Restriction enzymes are named after the bacterium from which they are isolated. For example, EcoRI is from Escherichia coli, and BamEII is from Bacillus amyloliquefaciens (Table 40-2). The first three letters in the restriction enzyme name consist of the first letter of the genus (E) and the first two letters of the species (co). These may be followed by a strain designation (R) and a roman numeral (I) to indicate the order of discov-ery (eg, EcoRI, EcoRIE). Each enzyme recognizes and cleaves a specific double-stranded DNA sequence that is 4—7 bp long. These DNA cuts result in blunt ends (eg,... 

Bacillus amyloliquefaciens, Streptomyces hygroscopicus Streptomyces hygroscopicus... 

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

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

Subtilisin (Bacillus amyloliquefaciens) 1 274 27 500 Bacterial proteolytic enzyme... 

Figure 11 (a) CI2 (magenta) from Hordeum sp. in complex with subtilisin novo (Bacillus amyloliquefaciens, cyan) shows the... 

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. 

Arrows indicate the phosphodiester bonds cleaved by each restriction endonuclease, Asterisks indicate bases that are methylated by the corresponding methylase (where known), N denotes any base. Note that the name of each enzyme consists of a three-letter abbreviation (in italics) of the bacterial species from which it is derived, sometimes followed by a strain designation and Roman numerals to distinguish different restriction endonucleases isolated from the same bacterial species, Thus BamHI is the first (I) restriction endonuclease characterized from Bacillus amyloliquefaciens, strain H. 

Various bacterial ribonucleases as well as the fungal ribonucleases Ty Uj, and U2 (see also Fig. 5-43) have amino acid sequences related to that of RNase A763 764 764a but with distinctly different three-dimensional structures. The active sites contain Glu, His, and Arg side chains. For RNase Ty Glu 58 and His 92 appear to provide acid-base catalysis with assistance from Tyr 38, Arg 77, and His 40.763 765 A glutamate carboxylate also appears to be the catalytic base in the related RNase, called barnase, from Bacillus amyloliquefaciens.766... 

The first crystal structure of a bacterial serine protease to be solved—subtilisin, from Bacillus amyloliquefaciens—revealed an enzyme of apparently totally different construction from the mammalian serine proteases (Figure 1.17). This was not unexpected, since there is no sequence homology between them. But closer examination shows that they are functionally identical in terms of substrate binding and catalysis. Subtilisin has the same catalytic triad, the same system of hydrogen bonds for binding the carbonyl oxygen and the acetamido NH of the substrate, and the same series of subsites for binding the acyl portion of... 

Bovine pancreatic RNase A is a member of a homologous superfamily. In addition, there is a separate family of guanine-specific microbial RNases that have evolved to have a similar active site.192,193 Ribonuclease T1 from Aspergillus oryzae and the 110-residue bamase from Bacillus amyloliquefaciens of Mr 12 392 (see Chapter 19) are the best known examples. One of the histidine residues is replaced by a glutamate in these enzymes. The microbial enzymes are much more amenable to study by protein engineering. 

Bamase (Figure 19.11), the 110-residue RNase that is secreted from Bacillus amyloliquefaciens, is of a + structure.50 It has a major a helix running from residues 6 to 18 (a helix, two smaller helixes in the first half of the sequence, and five strands of antiparallel sheet in the second half. There is a well-packed hydrophobic core formed by helixj packing onto one face of the sheet. All the peptidy 1-proline bonds are in the trans conformation. There are obvious regions... 

The serine proteases are divided into at least two genetic families the mammalian serine proteases, such as trypsin, chymotrypsin, elastase, the enzymes of the blood clotting system, and many other proteases with specific roles in control of systems and the bacterial proteases called subtilisins (first to be isolated from Bacillus amyloliquefaciens), which are genetically unrelated to the mammalian enzymes but independently evolved the same mechanism (evolutionary convergence). 

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... 

Another case, much more serious and also more pertinent to the chemical process development area, occurred in 1989 when over 1600 people became ill with eosinophilia-myalgia syndrome (EMS) and 38 died, worldwide, after taking l-tryptophan (Trp) manufactured by one producer in Japan. Prior to the outbreak, this producer whose Trp met the >98.5% purity specification had decided to employ a new genetically modified strain of the established Bacillus amyloliquefaciens and also to halve the amount of activated charcoal used in the purification step. These changes cause the Trp product to become contaminated with several new impurities, principally I to III, all associated to some extent (using a crude animal model) with EMS.5... 

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.

The application of a redox sensor in a control loop has been reported by Memmert and Wandrey [274] who controlled xylanase production of Bacillus amyloliquefaciens by defined oxygen limitation redox electrodes refer essentially to dissolved oxygen concentration below 10 mmol 1 102. This property was also promoted to determine the quality of anaerobic processes [403]. 

Restriction endonucleases are named in accordance with the proposals of Smith and Nathans (1973). Their names consist of a three letter abbreviation for the host organism (e.g. Eco for E. coli, Hin for Haemophilus influenzae. Bam for Bacillus amyloliquefaciens) followed by a strain designation and a Roman numeral. Thus Haemophilus influenzae, strain Rd contains at least three distinct restriction endonucleases and these are called Hindi, Hindll and Hindlll respectively. Restriction enzymes are generally known and described in the catalogues of suppliers by this code. 

Bacteria Bacillus subtilis Bacillus licheniformis Bacillus amyloliquefaciens... 

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