Abstract
Water-insoluble yeast invertase was pre-pared by binding native invertase to DEAE-cellulose. Some characteristics and continuous sucrose hydrolysis by this preparation were studied. (1) The activity of bound invertase cor-responded to about 1/2 of free invertase activity at pH 3.4. (2) Bound invertase perfectly hydrolyzed, sucrose into invert sugar as free invertase. (3) The apparent optimum pH of sucrose hydrolysis by bound invertase was 3.4. Whereas, optimum pH of free invertase was 5.4. (4) Bound invertase showed slightly less stability at pH 5.2 to the temperature in the range from 5°C to 40°C in comparison with free invertase. (5) Bound invertase showed higher stability to shaking at pH 3.6 in comparison with that at pH 5.4. (6) Continuous hydrolysis of sucrose by bound invertase was studied. Bound invertase could be used about ten times at pH 3.6 until the sucrose hydrolysis ratio decreased to the half of the initial.
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