[Purification and production of the extracellular 5-aminolevulinate from recombiniant Escherichia coli expressing yeast ALAS].

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He XM, Zhou J, Cheng Y, Fan J

[Purification and production of the extracellular 5-aminolevulinate from recombiniant Escherichia coli expressing yeast ALAS].

Sheng Wu Gong Cheng Xue Bao. 2007 May;23(3):520-4.

PubMed ID

17578005 [ View in PubMed

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Abstract

Aminolevulinic acid (ALA) is biosynthesized by the enzyme ALA synthase (ALAS). The ALA production has been studied using the overproducing ALAS from several bacteria in Escherchia coil, respectively. However, ALAS from eucaryote expressed in E. coli for producing ALA in the culture is not known. The extracellular ALA production and cell growth were investageted respectively using the recombinant E. coli overproducing Saccharomyces cerevisiae ALAS in shake-flask fermentations. The ALAS activity from the cell extract was assayed. The extracellular ALA was purified by the national-made large-dimension resins and confirmed by the capillary electrophoresis measurements. At 12h after induction at 37 degrees C, the extracellular ALA production was up to 162mg per liter LB culture at initial pH 6.5 with exogenous levulinate, succinate and and glycine at the concentration of 20 mmol/L respectively. The purity of ALA after purification is up to 90%.

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Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Glycine	5-aminolevulinate synthase, nonspecific, mitochondrial	Protein	Humans	Unknown	Substrate	Details