Effect of ultrasound on the activity of alliinase from fresh garlic

Alliinase is a homodimeric glycoprotein found most often in genus Allium plants. In this study, alliinase was purified from fresh garlic by using ammonium sulfate precipitation and gel filtration on a Sephacryl S-200 column. Homogeneity of the purified protein with a molecular weight of 54,000 Da was confirmed by SDS–PAGE. The effect of ultrasound on the alliinase activity was further studied. The optimal parameters for stimulating the alliinase activity were as follows: ultrasonic intensity, 0.5 W/cm2 and ultrasonic frequency, 40 kHz. Under the optimal conditions, ultrasonic irradiation did not affect the enzyme’s optimal temperature and pH, and improved its thermal stability. The low frequency and mild intensity ultrasound could increase the alliinase activity about 47.1%. Under ultrasound, the alliinase activity was inhibited by exogenous pyridoxal 5′-phosphate (PLP) and K+, and obviously enhanced by Fe2+. However, PLP and both of the metal ions showed opposite effects in the absence of ultrasound. Ultrasound could retard or slow down the inhibitory effect of l-cysteine on the alliinase activity. These results indicated that the activity of alliinase from fresh garlic might be enhanced by the low frequency and mild intensity ultrasound.