Enzymatic synthesis of S-phenyl-L-cysteine from keratin hydrolysis industries wastewater with tryptophan synthase

Bioresour Technol. 2013 Apr:133:635-7. doi: 10.1016/j.biortech.2013.02.011. Epub 2013 Feb 9.

Abstract

An economical method for production of S-phenyl-L-cysteine from keratin acid hydrolysis wastewater (KHW) containing L-serine was developed by recombinant tryptophan synthase. This study provides us with an alternative KHW utilization strategy to synthesize S-phenyl-L-cysteine. Tryptophan synthase could efficiently convert L-serine contained in KHW to S-phenyl-L-cysteine at pH 9.0, 40°C and Trion X-100 of 0.02%. In a scale up study, L-serine conversion rate reach 97.1% with a final S-phenyl-L-cysteine concentration of 38.6 g l(-1).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ammonium Chloride / pharmacology
  • Animals
  • Chromatography, Thin Layer
  • Cysteine / analogs & derivatives*
  • Cysteine / biosynthesis
  • Escherichia coli / enzymology
  • Fermentation / drug effects
  • Hydrogen-Ion Concentration / drug effects
  • Hydrolysis / drug effects
  • Industrial Waste / analysis*
  • Keratins / metabolism*
  • Serine / metabolism
  • Surface-Active Agents / pharmacology
  • Temperature
  • Tryptophan Synthase / metabolism*
  • Wastewater / chemistry*

Substances

  • Industrial Waste
  • Surface-Active Agents
  • Waste Water
  • Ammonium Chloride
  • beta-phenylcysteine
  • Serine
  • Keratins
  • Tryptophan Synthase
  • Cysteine