The Stability Improvement of α-Amylase Enzyme from Aspergillus fumigatus by Immobilization on a Bentonite Matrix

<table class="table-group" id="tab3"><tr><td><table class="table"><tr><td class="thead-hr" colspan="5"><hr/></td></tr><tr class="thead"><td class="align_left">Sample</td><td class="align_center">ki (min−1)</td><td class="align_center">t1/2 (min)</td><td class="align_center">ΔGi (kJ mole−1)</td><td class="align_center">Stability improvement</td></tr><tr><td class="thead-hr" colspan="5"><hr/></td></tr><tr><td class="align_left">Soluble enzyme</td><td class="align_center">0.0171 ± 0.0008</td><td class="align_center">40.53 ± 1.9001</td><td class="align_center">104.47 ± 0.1296</td><td class="align_center">1</td></tr><tr><td class="align_left">Immobilized enzyme</td><td class="align_center">0.0060 ± 0.0003</td><td class="align_center">115.50 ± 5.7895</td><td class="align_center">107.37 ± 0.1386</td><td class="align_center">2.9</td></tr><tr class="table-tr"><td colspan="5"><hr class="tbody-hr"/></td></tr></table></td></tr></table>

<div>ki, ΔGi, and t1/2 values for soluble and immobilized enzymes. The values are shown as mean ± SD, n = 2.</div>

Biochemistry Research International

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Table 3

Table 3: The Stability Improvement of α-Amylase Enzyme from Aspergillus fumigatus by Immobilization on a Bentonite Matrix