Behaviour of a recombinant cabbage (Brassica oleracea) phospholipase D immobilized on CNBr-activated and antibody supports.

Recombinant cabbage (Brassica oleracea) PLD2 (phospholipase D2) immobilized covalently on CNBr-activated Sepharose expressed low activity (approximately 10%), while that immobilized by binding on to anti-PLD2 IgG-Sepharose was more active (approximately 38%). Coupling of PLD2 to CNBr-activated Sepharose resulted in significant improvement in storage stability without affecting its thermostability, as compared with the soluble enzyme. Binding of PLD2 to the antibody support, however, rendered the enzyme remarkably labile to high temperatures and storage.