EXPRESSION OF PHENYLALANINE AMMONIA-LYASES IN ESCHERICHIA COLI STRAINS

被引：0

作者：

Kovacs, Klaudia ^{[1
,2
,3
]}

Holczinger, Andras ^{[4
]}

Vertessy, Beata ^{[3
,4
]}

Poppe, Laszlo ^{[1
,2
]}

机构：

[1] Budapest Univ Technol & Econ, Dept Organ Chem & Technol, H-1111 Budapest, Hungary

[2] HAS, Res Grp Alkaloid Chem, H-1111 Budapest, Hungary

[3] Hungarian Acad Sci, Inst Enzymol, H-1113 Budapest, Hungary

[4] Budapest Univ Technol & Econ, Dept Appl Biotechnol & Food Sci, H-1111 Budapest, Hungary

来源：

STUDIA UNIVERSITATIS BABES-BOLYAI CHEMIA | 2010年 / 55卷 / 04期

基金：

美国国家科学基金会;

关键词：

phenylalanine ammonia-lyase; heterologous protein expression; biocatalysis; phenylketonuria; TRANS-CINNAMIC ACID; GENE;

D O I：

暂无

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) catalyzes the non-oxidative conversion of L-phenylalanine into (E)-cinnamate. PAL can be applied in organic synthesis, and can be considered also for enzyme supplementation cure for genetic disorder phenylketonuria. The aim of this study was to find optimal expression parameters of several previously cloned PAL's (bacterial, plant and a chimera) in pBAD vectors for further functional characterization. Investigation of the expression level of PAL's in E. coli hosts with SDS PAGE analysis as well as activity assay of the recombinant PAL enzymes was performed.

引用

页码：275 / 282

页数：8

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