Preparation of optically active β-hydroxy-α-amino acid by immobilized Escherichia coli cells with serine hydroxymethyl transferase activity

@article{Zhao2010PreparationOO,
  title={Preparation of optically active β-hydroxy-α-amino acid by immobilized Escherichia coli cells with serine hydroxymethyl transferase activity},
  author={Gen-Hai Zhao and Hui Li and Wei Liu and Weiguo Zhang and Fei Zhang and Qian Liu and Qing-cai Jiao},
  journal={Amino Acids},
  year={2010},
  volume={40},
  pages={215-220}
}
In this research, an improved method for preparation of optically pure β-hydroxy-α-amino acids, catalyzed by serine hydroxymethyl transferase with threonine aldolase activity, is reported. Using recombinant serine hydroxymethyl transferase (SHMT), an enzymatic resolution process was established. A series of new substrates, β-phenylserine, β-(nitrophenyl) serine and β-(methylsulfonylphenyl) serine were used in the resolution process catalyzed by immobilized Escherichia coli cells with SHMT… CONTINUE READING
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Immobilization of a recombinant Escherichia coli producing a thermostable a-L-rhamnosidase: Creation of a bioreactor for hydrolyses of naringin

  • H Birgisson, JO Wheat, GO Hreggvidsson, JK Kristjansson, B Mattiasson
  • Enzyme Microb Tech
  • 2007
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