PRONASE IMMOBILIZED ON POLY(N-ACRYLOYLPIPERIDIN-4-ONE) - A L-ENANTIOSPECIFIC HYDROLYSIS OF ALPHA-AMINONITRILES WITH IMMOBILIZED AMIDASE

Citation
J. Taillades et al., PRONASE IMMOBILIZED ON POLY(N-ACRYLOYLPIPERIDIN-4-ONE) - A L-ENANTIOSPECIFIC HYDROLYSIS OF ALPHA-AMINONITRILES WITH IMMOBILIZED AMIDASE, Bulletin de la Societe chimique de France, 132(1), 1995, pp. 119-127
Citations number
22
Categorie Soggetti
Chemistry Inorganic & Nuclear",Biology,Chemistry
ISSN journal
00378968
Volume
132
Issue
1
Year of publication
1995
Pages
119 - 127
Database
ISI
SICI code
0037-8968(1995)132:1<119:PIOP-A>2.0.ZU;2-5
Abstract
Pronase immobilized on poly(N-acryloylpiperidin-4-one) : a L-enantiosp ecific hydrolysis of alpha-aminonitriles with immobilized amidase. alp ha-Aminonitriles are not substrates for pronase (an amidase) in the ho mogeneous phase but become substrates for pronase when it is immobiliz ed on polymer matrix with ketonic sites (piperidin-4-one). In this pap er we show that under low basic aqueous conditions (pH 10-11). the hyd ration of alpha-aminonitriles can be efficiently catalyzed by poly(N-a cryloylpiperidin-4-one) crosslinked with 1,4-bis acryloylpiperazine (A (80:20) in the presence of phosphate or berate buffers. These conditio ns comply with the hydrolysis of alpha-aminoamides by pronase immobili zed on poly(N-acryloylpiperidin-4-one) crosslinked with 1,4-bis(acrylo yl)piperazine (A(80:20/p). Thus, in a buffered berate solution at pH 1 0.5, alpha(DL)-aminonitrile is enantiospecifically hydrolyzed into alp ha(D)-aminoamide and alpha(L)-amino acid.