Library Growth and Protein Expression: Optimal and Reproducible Microtiter Plate Expression of Recombinant Enzymes in E. coli Using MTP Shakers

We developed a protocol for an optimal and reproducible protein expression in microtiter plates showcased for the expression of the cyclohexanone monooxygenase from Acinetobacter sp

Sandy Schmidt

2017

Scholarcy highlights

  • Escherichia coli as heterologous host enables the recombinant expression of the desired protein in high amounts
  • The expression of different enzyme variants often leads to a diverse growth behavior of the E. coli clones resulting in the identification of false-positives when screening a mutant library
  • We developed a protocol for an optimal and reproducible protein expression in microtiter plates showcased for the expression of the cyclohexanone monooxygenase from Acinetobacter sp
  • Our optimized protocol provides a comprehensive overview of the key factors influencing a reproducible protein expression and this should serve as basis for the adaptation to other enzyme classes
  • Biotechnol Bioeng 80:42–49CrossRefPubMedGoogle Reactor operation and scale-up of whole cell Baeyer-Villiger catalyzed lactone synthesis

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