Purification and properties of D-hydantoin hydrolase and N-carbamoyl-D-amino acid amidohydrolase from Flavobacterium sp AJ11199 and Pasteurella sp AJ11221

被引：10

作者：

Nozaki, H ^{[1
]}

Kira, I ^{[1
]}

Watanabe, K ^{[1
]}

Yokozeki, K ^{[1
]}

机构：

[1] Ajinomoto Co Inc, Animosci Labs, Kawasaki Ku, Kawasaki, Kanagawa 2108681, Japan

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2005年 / 32卷 / 5-6期

关键词：

D-hydantoin hydrolase; N-carbamoyl-D-amino acid amidohydrolase; Flavobacterium; Pasteurella;

D O I：

10.1016/j.molcatb.2004.12.003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We characterized recombinant D-hydantoin hydrolase (DHHase) and N-carbamoyl-D-amino acid amidohydrolase (DCHase) from Flavobacterium sp. AJ11199 and Pasteurella sp. AJ11221. The DHHases from these two strains showed a wide range of hydrolytic activity for various 5-monosubstituted D-hydantoin compounds, including a very high level activity for D-hydantoin compounds corresponding to D-aromatic amino acids such as D-tryptophan D-phenylalanine and D-tyrosine. The DCHases, in turn, were capable of catalyzing the hydrolysis of various N-carbamoyi-D-amino acids (NCD-A.A.) corresponding to D-aliphatic and D-aromatic amino acids. The combination of these enzymes was found to be applicable for the production of various D-amino acids. (c) 2004 Elsevier B.V. All rights reserved.

引用

页码：205 / 211

页数：7

共 14 条

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