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Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli

Park, J.-S.; Han, K.-Y.; Song, J.-A.; Ahn, K.-Y.; Seo, H.-S.; Lee, J.

Biotechnology Letters 29(10): 1513-1518

2007


ISSN/ISBN: 0141-5492
PMID: 17549433
DOI: 10.1007/s10529-007-9417-3
Accession: 015725841

Using 2-dimensional gel electrophoresis, the Escherichia coli proteome response to a heat-shock stress was analyzed and a 1.6-fold increase of malate dehydrogenase was observed even under the heat-shock condition where the total number of soluble proteins decreased by about 5%. We subsequently demonstrated that, as an N-terminus fusion expression partner, malate dehydrogenase facilitated the folding of, and dramatically increased the solubility of, many aggregation-prone heterologous proteins in E. coli cytoplasm. Therefore, malate dehydrogenase is well suited for production of a biologically active fusion mutant of cutinase (Pseudomonas putida origin) that is currently of considerable to biotechnology and commercial industries.

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