Temperature affects soluble recombinant protein yield in E. coli.

the verdict

INSUFFICIENT LEANING

Recorded sources

6 sources for · 0 against

Counts group repeated records of the same source within each side. They do not measure evidence strength or source independence.

Is it true that temperature affects soluble recombinant protein yield in E. coli?

Unclear. Several individual E. coli expression studies report that lowering cultivation or induction temperature increased the soluble fraction of specific recombinant proteins, though each covers only one protein system and the effect is often partial. No single item establishes the general claim across all recombinant proteins.

Verdict: PARTIAL LEAN · 6 sources for, 0 against · Last checked 18 Oct 2026

The private library was unavailable for some searches in this check. Missing library results are not evidence against the claim.

Evidence for · 6

Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli

1997

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Weickert, M. J., Pagratis, M., Curry, S. R., & Blackmore, R. (1997). Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli. doi.org. https://doi.org/10.1128/aem.63.11.4313-4320.1997

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More for · 5

Purification and characterization of a soluble recombinant human ST6Gal I functionally expressed in Escherichia coli

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Purification and characterization of a soluble recombinant human ST6Gal I functionally expressed in Escherichia coli. (n.d.). cir.nii.ac.jp. https://doi.org/10.1007/s10719-005-0845-9

Production of high levels of soluble recombinant Streptomyces clavuligerus isopenicillin N synthase in Escherichia coli

1996

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Production of high levels of soluble recombinant Streptomyces clavuligerus isopenicillin N synthase in Escherichia coli. (1996). doi.org. https://doi.org/10.1016/s1381-1177(96)00019-7

Recombinant expression of natural Arabidopsis PRLIP1 variants reveals temperature-dependent differences in fluorescence and functional protein recovery in Escherichia coli.

2026

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G, M., S, K., & G, J. (2026). Recombinant expression of natural Arabidopsis PRLIP1 variants reveals temperature-dependent differences in fluorescence and functional protein recovery in Escherichia coli.. doi.org. https://doi.org/10.1007/s11274-026-05138-y

Recombinant production of ESAT-6 antigen in thermoinducible Escherichia coli: the role of culture scale and temperature on metabolic response, expression of chaperones, and architecture of inclusion bodies

2019

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Recombinant production of ESAT-6 antigen in thermoinducible Escherichia coli: the role of culture scale and temperature on metabolic response, expression of chaperones, and architecture of inclusion bodies. (2019). doi.org. https://doi.org/10.1007/s12192-019-01006-x

Cytoplasmic Chaperones Enhance Soluble Expression of Anti-EGFR huscFv in Escherichia coli.

2020

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Cytoplasmic Chaperones Enhance Soluble Expression of Anti-EGFR huscFv in Escherichia coli.. (2020). doi.org. https://doi.org/10.30498/ijb.2020.138200.2314

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held for human review18 Oct 2026

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