Comparative Investigation of Glutathione S-Transferases, Glyoxalase-I and Alliinase Activities in Different Vegetable Crops

Glutathione S-transferases (GSTs, EC 2.5.1.18), glyoxalase-I (EC 4.4.1.5) and alliin lyase (alliinase, EC 4.4.1.4) are important enzyme sys-tems in plant bodies. The first two are mainly detoxifying enzymes that utilize glutathione (GSH) in the defense mechanism, and the last one is mainly involved in secondary metabolism and relevant to sulfur compounds derived from GSH. The activities of the three enzymes have been investigated in soluble extracts of vegetable crops, including pumpkin, cabbage, broccoli, radish, carrot, potato, sweet potato, mungbean, and onion. GST activities were detected in all of the vegetables, and the extract of onion bulb exhibited the highest specific activity (648 nmol/min/mgP). The putative GSTs of most of the vegetables were found to be induced by ethanol. The activities of GSTs in onion bulb were found to be markedly inhibited by S-hexyl glutathione and were also inhibited by S-butyl glutathione and S-propyl glutathione. The anti-CmGSTF1 antiserum recognized a thick band for putative onion GST. The estimated glyoxalase-I activity level was also high in onion bulb (4540 nmol/min/mgP), indicating that the thick band detected by Western blot analysis might result from partial recognition of glyoxalase-I by the antiserum. The specific activities for glyoxalase-I were moderate in radish and carrot, and the extracts of other vegetables had rather low lev-els of activities. The extract of onion also showed the highest specific activity level for alliinase (2069nmol pyruvate/mgP). The extracts of other vegetables also had alliinase activities, although the estimated values were much lower than that of onion