Nitrilasic activity of a resin amidase immobilized on poly(N-acryloylpiperidin-4-one)

In this paper, we show that the l-enantiospecific hydrolysis of d,l-α-aminonitriles into l-α-amino acids is catalyzed by an amidase (pronase) immobilized on poly(N-acryloylpiperidin-4-one). Actually, the support chemically participates in the catalytic action since the ketonic sites (piperidin-4-one) catalyze the d,l-α-aminonitrile hydration into d,l-α-aminoamide in a medium specifically buffered by borates or phosphates at pH 10–11. These conditions are compatible with the enzymatic activity of the pronase and allow the simultaneous transformation of the d,l-α-aminoamide formed in the resin into the corresponding l-α-amino acid.