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

J. Taillades, L. Garrel, F. Guillen, H. Collet, A. Commeyras
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引用次数: 1

Abstract

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.

固定化聚(n-丙烯酰胡椒苷-4- 1)树脂酰胺酶的硝化活性
在本文中,我们证明了d, 1 -α-氨基腈的l-对映体特异性水解为1 -α-氨基酸是由固定在聚(n-丙烯酰哌啶-4- 1)上的酰胺酶(pronase)催化的。实际上,在pH值为10-11的硼酸盐或磷酸盐缓冲介质中,酮位(哌替啶-4-酮)催化d, 1 -α-氨基腈水化成d, 1 -α-氨基酰胺,因此载体在化学上参与了催化作用。这些条件与蛋白酶的酶活性相适应,并允许树脂中形成的d,l-α-氨基酰胺同时转化为相应的l-α-氨基酸。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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