Enhancement of soluble expression of codon-optimized Thermomicrobium roseum sarcosine oxidase in Escherichia coli via chaperone co-expression
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文摘

Based on whole-genome analysis of T. roseum DSM 5159, the codon-optimized sox was successfully expressed in E. coli.

The soluble expression of SOX was significantly enhanced via co-expression of chaperones (GroES-GroEL and DnaK-DnaJ-GrpE-GroES-GroEL).

Analysis of intermolecular forces indicated that Arg, hydrogen bonds, and ionic bonds enhanced the interactions and stability of the TrSOX secondary structures.

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