ABSTRACT
The influence of physicochemical conditions on the phospholipase D (PLD) activity of subcellular preparations of sweet corn (Zea mays L. cv. Peaches and Cream) kernels has been studied. The microsomal, mitochondrial, and cytosolic preparations of corn kernels possessed PLD activity albeit at varying proportions. The microsomal and cytosolic PLD activities were stimulated 2-fold between 5 and 15 degrees C. Ethanol had varying modulatory effects on PLD activity. By contrast, acetaldehyde was a potent inhibitor of PLD. As well, a naturally occurring C(6) aldehyde such as hexanal and an alcohol such as hexanol inhibited PLD activity efficiently. Divalent cations such as calcium chloride and magnesium chloride stimulated PLD activity at micromolar levels. Monovalent cations such as KCl and NaCl did not appear to affect PLD activity. Partial purification of PLD from the microsomal, mitochondrial, and cytosolic fractions separately revealed four major isoforms with relative molecular masses of 200, 140-150, 102-108, and 60-66 kDa. The importance of PLD in the maintenance of processed food quality is discussed.
Subject(s)
Food Handling , Phospholipase D/metabolism , Subcellular Fractions/enzymology , Zea mays/enzymology , Cytosol/enzymology , Hydrogen-Ion Concentration , Microsomes/enzymology , Phospholipase D/isolation & purification , Temperature , Zea mays/ultrastructureABSTRACT
The potential role of antioxidant enzymes in protecting maize (Zea mays L.) seedlings from chilling injury was examined by analyzing enzyme activities and isozyme profiles of chilling-susceptible (CO 316) and chilling-tolerant (CO 328) inbreds. Leaf superoxide dismutase (SOD) activity in CO 316 was nearly one-half that of CO 328, in which the high activity was maintained during the chilling and postchilling periods. Activity of glutathione reductase (GR) was much higher in roots than in leaves. CO 328 also possessed a new GR isozyme that was absent in roots of CO 316. Ascorbate peroxidase (APX) activity was considerably lower in leaves of CO 328 than in CO 316, and nearly similar in roots. Paclobutrazol treatment of CO 316 induced several changes in the antioxidant enzyme profiles and enhanced their activities, especially those of SOD and APX, along with the induction of chilling tolerance. These results suggest that increased activities of SOD in leaves and GR in roots of CO 328, as well as SOD and APX in leaves and roots of paclobutrazol-treated CO 316, contribute to their enhanced chilling tolerance.
