Comparative studies on a mesophilic and a thermophilic alpha-amylase.
A comparative study was performed on thermal stability of mesophilic and thermophilic alpha-amylases, and the effects of various denaturing agents, organic solvents, and stabilizers were investigated. As expected, the thermophilic enzyme showed higher resistance toward denaturation in water as its natural medium, but such a difference could not be detected in nonaqueous environments. Furthermore, stability of these molecules was improved by including various stabilizing agents. Of the compounds tested, sorbitol provided the highest degree of protection, which was found to be owing to its effect on increasing Tm and its ability in totally preventing deamidation of amino acid residues in the protein molecules.
Institute of Biochemistry and Biophysics, University of Tehran, PO Box 13145-1384, Tehran, Iran.
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Khajeh
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Nemat-Gorgani
D001407:Bacillus / Q000201:enzymology; D003902:Detergents / Q000378:metabolism; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D011489:Protein Denaturation; D012997:Solvents; D013012:Sorbitol / Q000378:metabolism; D013816:Thermodynamics; D014867:Water / Q000378:metabolism; D000516:alpha-Amylases / Q000737:chemistry* / Q000378:metabolism*
D003902:Detergents; D012997:Solvents; D014867:Water; D013012:Sorbitol; D000516:alpha-Amylases