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    		 BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE                             

Alpha amylase or a-(1,4)-glucan-4-glucanohydrolase, is an enzyme that catalyzes the hydrolysis of a-D-(1,4)-glucosidic linkages in starch and other related carbohydrates. The enzyme from Bacillus Stearothermophilus is thermo-stable and is found to be active at 75C for about 50 min.  It undergoes irreversible thermo-inactivation at 90C. Due to these properties, this enzyme finds wide applications in the textile industry for removal of starch in a process called de-sizing. The cotton fibers are starched before they are weaved to give them enough tensile strength to withstand weaving. After, that they have to be de-starched or "de-sized" before further use. Treatment with a thermo-stable enzyme that specifically removes starch without damaging the material would be an ideal step in this process. The alpha amylase characterized here could be a potential candidate for such industrial applications. 

The three dimensional structure of shows that it consists of a single polypeptide chain folded into three distinct domains as observed commonly in most alpha-amylases. As compared to other amylases, this enzyme has some voids in the alpha helical region close to the active site that decrease their hydrophobic interactions and the inter-helical compactness. They also have fewer hydrogen bonds near the active site that could also contribute to the decreased thermo-stability. It has also been calculated that the solvent-ASA of the charged residues is almost half as compared to other amylases that could affect the thermo-stability of the enzyme. Even though it is not as stable as B. amyloliquefaciens alpha-amylase (90C, pH 6.5 and 270 min.) it is ideal for industrial applications because at its temperature optima it doesn't undergo thermo-inactivation.

This enzyme acts on polysaccharides and hence has multiple binding sites for the polymers. Apart from the active site where the cleavage takes place, they have extended substrate-binding sites to anchor the polysaccharide. The Ca-Na-Ca metal triad found in these enzymes act as stabilizing sites for the polysaccharides. Studies on the triad show that the Sodium atom is responsible for the stability and in some cases they can diffuse in and out of the molecule. It has also been shown in alpha amylases from similar organisms that there is a specific orientation of the metal triad and a potentially a cis-peptide bond could be involved in the binding pocket.

References:
Crystal Structure of Bacillus Stearothermophilus a-amylase: Possible factors determining the thermostability 
Duvjir Suvd et al, J. Biochem. Vol.129, pp. 461-468 (2001).      

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Domain A is the compact core structure with a (b/a)8- barrel.  Domain B consists of a sheet of four anti-parallel beta sheets with long loops between the beta sheets.  Domain C contains 8 beta strands folded into a Greek key motif forming the globular unit. 
View 1 shows the b/a barrel of Domain A very clearly with the active site of the molecule in the center.
View 2 shows all the three distinct domains with the beta sheet of domain C in the left corner followed by the beta-alpha barrel of Domain A and the globular Domain C subunit.
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