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

✍ Scribed by J. Taillades; L. Garrel; F. Guillen; H. Collet; A. Commeyras

• Book ID: 103956642
• Publisher: Elsevier Science
• Year: 1995
• Weight: 649 KB
• Volume: 24
• Category: Article
• ISSN: 0923-1137
• DOI: 10.1016/0923-1137(94)00092-j

✦ Synopsis

In this paper, we show that the L-enantiospecific hydrolysis of D,L-a-aminonitriles into L-a-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-a-aminonitrile hydration into D,L-a-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-a-aminoamide formed in the resin into the corresponding L-a-amino acid.