Optimization of D-amino acid production catalyzed by immobilized multi-enzyme system in polyelectrolyte complex gel capsules

被引:11
|
作者
Aranaz, I. [1 ,2 ]
Acosta, N. [1 ,2 ]
Fernandez-Valle, M. E. [1 ,2 ]
Heras, A. [1 ,2 ]
机构
[1] Univ Complutense, Fac Farm, Inst Estudios Biofunc UCM, Dept Fis Quim 2, Madrid 28040, Spain
[2] Univ Complutense, CAI RMN, Madrid 28040, Spain
关键词
p-Hydroxyphenylglycine; Encapsulation; D-Hydantoinase; N-carbamyl-D-amino acid amydohydrolase; Alginate; Chitosan; Magnetic resonance imaging; D-P-HYDROXYPHENYLGLYCINE; D-HYDANTOINASE; ESCHERICHIA-COLI; ENZYMES; AMIDOHYDROLASE; CARBAMOYLASE; STABILITY; RESIDUES; CHITOSAN;
D O I
10.1016/j.molcatb.2015.06.003
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
Multi-enzyme systems containing D-hydantoinase and D-carboamylase encapsulated in alginate-chitosan polyelectrolyte complexes have been proved as interesting biocatalysts to produce D-p-hydroxyphenylglycine. These biocatalysts were produced in a one-step procedure (so called biocatalyst V-I) and in a two-step procedure (so called biocatalyst V-II). In this paper, the production of D-p-hydroxyphenylglycine by using these biocatalysts is optimized taking into account the special features of this system (low enzyme stability and both substrate poor solubility and low stability with temperature). The best operational conditions to produce D-p-hydroxyphenylglycine are identified. Moreover, the encapsulation allows us to carry out the reaction in heterogeneous conditions and to reuse the biocatalysts 3 and 5 times without losing their activity for biocatalyst V-II and V-I, respectively. Finally, the encapsulation dramatically protects the enzymatic activity during lyophilization improving biocatalysts storage. (C) 2015 Published by Elsevier B.V.
引用
收藏
页码:45 / 52
页数:8
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