Co-immobilization of D-hydantoinase and D-carboamylase on Chitin: Application to the Synthesis of p-hydroxyphenylglycine

被引：26

作者：

Aranaz, I

Ramos, V

De La Escalera, S

Heras, A

机构：

[1] Univ Complutense, Inst Estudios Biofunc, Fac Farm, Dept Fis Quim 2, E-28040 Madrid, Spain

[2] Univ Nacl Sur, Dept Quim & Ingn Quim, RA-8000 Bahia Blanca, Buenos Aires, Argentina

来源：

BIOCATALYSIS AND BIOTRANSFORMATION | 2003年 / 21卷 / 06期

关键词：

Agrobacterium radiobacter; chitin; co-immobilization; D-Hydantoinase; N-Carbamyl-D-Amino acid Amidohydrolase;

D O I：

10.1080/10242420310001597829

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The immobilization of a multi-enzyme extract is an excellent method for multi-step biotransformations. This paper describes how a multi-enzyme extract from Agrobacterium radiobacter , rich in d -hydantoinase and N-carbamyl- d -amino acid amidohydrolase was immobilized on chitin for its application on the synthesis of p-hydroxyphenylglycine. The adsorption derivative showed a higher activity than the covalent one. Compared to the soluble multi-enzymatic extract, the adsorption derivative showed greater pH-stability in the pH range under study. Its optimum pH ranged from 7-8. Furthermore, it showed high activity at low temperature.

引用

页码：349 / 356

页数：8

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