Abstract
An acid protease from Aspergillus saitoi was immobilized on agarose beads of approximately 100 micrometers diameter. Solutions of gelatin were prepared in a saturated potassium bitartrate buffer and contacted with the immobilized enzyme. The Michaelis-Menten constant was determined to be 7.8 x 10-5 M at 25°C and pH of 3.5.
The maximum velocity of hydrolysis corrected for bed voidage was found to be 6.8 x 10-7 M per second under the same conditions.
- Received September 1980.
- Revision received November 1980.
- Accepted November 1980.
- Published online January 1981
- Copyright 1981 by the American Society for Enology and Viticulture
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Vol 32 Issue 1
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