A-Amylase Bacillus subtilis

Takeda, Y., Hizukuri, S., Ozono, Y., and Suetake, M. 1983. Actions of porcine pancreatic and Bacillus subtilis a-amylase and Aspergillus niger glucoamylase on phosphorylated (l- 4)-a-D-giucan. Biochim Biophys. Acta 749, 302-311. 

The various a-amylases contain, per mole, at least one gram-atom of firmly bound calcium, which is required both for enzymic activity and to prevent destruction of the amylases by proteolytic enzymes. Bacillus subtilis a-amylase is unusual in that it also contains small proportions of zinc and exists as a dimer which is crosslinked by a zinc atom. Removal of the zinc does not inactivate the enzyme. 

The action of Bacillus subtilis a-amylase on 6-O-methylamylose and 6-deoxyamylose has been investigated, the products being characterized by mass spectrometry. A modified D-glucose monomer was not found in any of the... 

Taka amylase a bacterial a-amylase (EC 3.2.1.1) isolated and crystallized from Aspergillus oryzae taka diastase preparations. T. a. (Af, 50,000) is a calcium-containing, single-chain protein with V-terminal alanine and C-terminal serine. Like the tetrameric Bacillus subtilis a-amylase (Af, 96,000), T.a. is resistant to sodium dodecylsulfate but is reversibly denatured by 6 M guanidine or 8 M urea. T.a. must not be confused with Adenosine deaminase (see), which is also present in taka diastase. 

Photo-control of the enzymic activity has been achieved by attaching a photo-chromic spiropyran to a-amylase. The derivative obtained when Bacillus subtilis a-amylase reacted with l-(2-carboxyethyl)-3,3-dimethyl-6 -nitrospiro[indoline-2,2 -2//-benzopyran] anhydride exhibited a reversible photochromism in aqueous solution it is yellow in the dark and colourless under u.v.-irradiation. The enzymic activity of the colourless derivative is much less than that of the coloured derivative, due, most probably, to a change in affinity for the substrate (amylose). 

A j8-D-glucanase highly specific for jS-D-glucans containing a linkage sequence (13) has been isolated from several commercial preparations of Bacillus subtilis a-amylase including one purified by repeated crystallization. The... 

M. and Tamura, G., 1984, Secretion vector of Bacillus subtilis constructed from the Bacillus subtilis a-amylase promoter and signal peptide coding region, "Genetics and Biotechnology of Bacilli", A.T. Ganasan and J.A. Hoch, eds.. Academic Press, London and Orlando, pp. 181. 

Mouse immunoglobulin anti- Bacillus subtilis a-amylase) antibody Removal of cross-reacting materials from modified B. subtilis a-amylase by immunoadsorption 57 ... 

Acetylation of a tyrosyl residue in Bacillus subtilis amylase led to partial loss of the enzymic activity towards a series of malto-oligosaccharides, indicating that a tyrosyl residue located near the catalytic site is involved in the productive binding of substrates. The difference spectrum of a tryptophanyl residue in Bacillus subtilis a-amylase was significantly decreased following treatment with... 

A -bromosuccinimide. Immune responses to a heavy conjugate of Bacillus subtilis a-amylase and 4-diazoquinoIine 1-oxide have been examined. ... 

Bacillus subtilis a-amylase immobilized on a phenol-formaldehyde resin displayed exo-activity, which might result from steric hindrance between the immobilized enzyme and substrates of high molecular weight (e.g. amylopectin). Thus, cleavage of the peripheral D-glucosidic linkages produced small oligosaccharides only. 

Grauwet, T., van der Plancken, L, VervoorL L., Hendrickx, M., and van Loey, A. (2009) Investigating the potential of Bacillus subtilis a-amylase as a pressure-temperature-time indicator for high hydrostatic pressure pasteurization processes. Biotechnology Progress, 25, 1184-1193. 

Bacillus subtilis a-amylase which contains no disulfide linkage has been denatured in 8 M urea under acidic conditions. The reversibility of the process after removal of the denaturant was shown by the return of the optical properties (ORD and UV absorption) and also by the return of the enzymatic activity (Fukushi et al., 1963). 

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