Journal
BIOLOGIA
Volume 77, Issue 3, Pages 893-905Publisher
SPRINGER
DOI: 10.1007/s11756-021-00994-5
Keywords
Escherichia coli; Heterologous expression; Soluble production; Fusion tags; Chaperones
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This review focuses on various strategies to enhance the soluble yield of active recombinant proteins, including the choice of vector, host strain, culturing conditions, use of various fusion tags and chemical or biological chaperones.
Escherichia coli is the first choice host for heterologous production of recombinant proteins with high yield due to its robust and economical growth. However, occasionally recombinant proteins are either not produced or produced in misfolded, insoluble and inactive form. In this review we focus on various strategies to enhance the soluble yield of active recombinant proteins by exploring the choice of vector, host strain, culturing conditions, use of various fusion tags and chemical or biological chaperones for soluble production of heterologous proteins.
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