Role of environment on the activity and stability of α-amylase incorporated in reverse micelles |
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Authors: | Claudia Shah Subramani Sellappan Datta Madamwar |
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Affiliation: | (1) Post Graduate Department of Biosciences, Vallabh Vidyanagar-388 120, Gujarat, India |
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Abstract: | ![]() α-amylase (3.2.1.1) was solubilized in reverse micelles formed by Triton X-100 in xylene. Although the enzyme shows decrease in specific activity in reverse micellar medium, it possesses significantly high stability in comparison to bulk aqueous medium. Water/Surfactant ratio (Wo) was found to play a crucial role in both activity and stability of the enzyme. The optimum water/surfactant ratio for the catalytic function of an enzyme in reverse micelles is 36, while the enzyme is stable at Wo 12 for a considerably long period, and at Wo above 20 the enzyme gets inactivated within a day. Glycerol and CaCl2 improve the stability in both aqueous and reverse micellar medium. Thus the interior of the reverse micelles acts as a microreactor and provides favorable environment for the enzyme activity and stability. |
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Keywords: | α -Amylase reverse micelles Triton X-100 xylene water/surfactant ratio glycerol CaCl2 |
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