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Temperature-induced production of recombinant human insulin in high-cell density cultures of recombinant Escherichia coli.

Abstract：

:The construction of expression vectors encoding either the human insulin A- or B-chains fused to a synthetic peptide and the temperature-induced expression of the recombinant genes in Escherichia coli are reported. Using this two-chain approach we also describe the separate isolation of the insulin A- and B-chains from inclusion bodies and their subsequent assembly into native human insulin. The production of the insulin fusion proteins were carried out in high-cell density fed-batch cultures using a synthetic medium with glucose as sole carbon and energy source. The expression of the recombinant genes by temperature-shift in high-cell density cultures of recombinant E. coli resulted in product yields of grams per litre of culture broth, e.g. 4.5 g of insulin B-chain fusion protein per litre of culture broth. This translates into an expression yield of about 800 mg of the insulin B-chain per litre of culture. Under similar cultivation conditions the expression yield of the insulin A-chain corresponds to approximately 600 mg per litre of culture. The metabolic burden imposed on the recombinant cells during temperature-induced production of insulin fusion proteins in high-cell density cultures is reflected in an increased respiratory activity and a reduction of the biomass yield coefficient with respect to glucose.

journal_name

J Biotechnol

journal_title

Journal of biotechnology

authors

Schmidt M,Babu KR,Khanna N,Marten S,Rinas U

doi

10.1016/s0168-1656(98)00189-8

subject

Has Abstract

pub_date

1999-02-05 00:00:00

pages

71-83

issue

1

eissn

0168-1656

issn

1873-4863

pii

S0168165698001898

journal_volume

68

pub_type

杂志文章

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