The Study of an Immobilized Acid Protease for the Treatment of Wine Proteins

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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.

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