%0 Journal Article %A Alan T. Bakalinsky %A Roger Boulton %T The Study of an Immobilized Acid Protease for the Treatment of Wine Proteins %D 1985 %R 10.5344/ajev.1985.36.1.23 %J American Journal of Enology and Viticulture %P 23-29 %V 36 %N 1 %X 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. %U https://www.ajevonline.org/content/ajev/36/1/23.full.pdf