3.3. Characterization of the beta a

3.3. Characterization of the beta amylase immobilized onglutaraladehyde agarose beadsThe goal of these experiments was not to find the optimalconditions for the different enzyme preparations, but to show afirst comparison between the immobilized and the free enzyme.Fig. 1A shows the effect of pH on activity of free and immobilizedbeta-amylase. Both preparations have better results when citrate-phosphate buffer was used, but the free enzyme presented optimalpH value at pH 6.0, while the immobilized amylase had a maximumactivity at pH 6.5. Roy and Edge [33] also observed an increase inthe optimum pH, from 5.0 to 5.6. Very interestingly, the immobi-lized amylase maintained high activity in all the range of pH valuesstudied, even in the most extreme ones (pH 3.0, and 10.0), whilethe free enzyme dramatically decreased its activity by just moving