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).
Copyright © 2013 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Ammonium Chloride / pharmacology
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Animals
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Chromatography, Thin Layer
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Cysteine / analogs & derivatives*
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Cysteine / biosynthesis
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Escherichia coli / enzymology
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Fermentation / drug effects
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Hydrogen-Ion Concentration / drug effects
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Hydrolysis / drug effects
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Industrial Waste / analysis*
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Keratins / metabolism*
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Serine / metabolism
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Surface-Active Agents / pharmacology
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Temperature
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Tryptophan Synthase / metabolism*
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Wastewater / chemistry*
Substances
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Industrial Waste
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Surface-Active Agents
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Waste Water
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Ammonium Chloride
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beta-phenylcysteine
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Serine
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Keratins
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Tryptophan Synthase
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Cysteine