Abstract
A food-grade acid protease was successfully immobilized on derivatized agarose beads 100 microns in diameter. The immobilized protease retained 16% of the activity of its original, soluble counterpart. Its half-life, while stored in a solution consisting of 12% ethanol, 0.6% potassium bitartrate, 200 mg/L sodium azide at pH 3.0 and 37°C was determined to be 57 hours. The apparent Michaelis constant (K'm) and the apparent maximum velocity (V'max) in a model system composed of Hammarsten casein in 0.6% potassium bitartrate at pH 3.0 and 37°C were 0.65 g dry weight casein/L and 4.8 x 10-5 moles glycine equivalents/L [unknown] min [unknown] g dry weight conjugate, respectively. The activity versus temperature profile of the enzyme-agarose conjugate differed slightly from that of the original soluble protease. One of four heat-unstable wines treated with the conjugate in a recirculating-flow packed-bed reactor was stabilized.
- Received April 1984.
- Copyright 1985 by the American Society for Enology and Viticulture
Sign in for ASEV members
ASEV Members, please sign in at ASEV to access the journal online.
Sign in for Institutional and Non-member Subscribers
Log in using your username and password
Pay Per Article - You may access this article (from the computer you are currently using) for 2 day for US$10.00
Regain Access - You can regain access to a recent Pay per Article purchase if your access period has not yet expired.