Production of S-(carboxymethyl)-l-cysteine from l-serine with tryptophan synthase
| Autor: | Nakamura Takeshi, Nobuyoshi Makiguchi, Masao Shimada, Kenichi Ishiwata |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
musculoskeletal diseases
chemistry.chemical_classification biology Stereochemistry technology industry and agriculture Tryptophan synthase macromolecular substances musculoskeletal system medicine.disease_cause Applied Microbiology and Biotechnology Tryptophan synthase activity body regions Serine Hydrolysis chemistry.chemical_compound Enzyme chemistry biology.protein medicine Organic chemistry Thioglycolic acid Escherichia coli Biotechnology Cysteine |
| Zdroj: | Journal of Fermentation and Bioengineering. 68:84-87 |
| ISSN: | 0922-338X |
| DOI: | 10.1016/0922-338x(89)90052-4 |
| Popis: | Synthesis of S -carboxymethyl)- l -cysteine ( l -CMC) from L-serine with tryptophan synthase was studied. In the β-replacement reaction l -serine catalyzed by tryptophan synthase of Escherichia coli , thioglycolic acid was a poor substrate but alkylthioglycolates were good substrates. S -(2-Ethylhexyloxycarbonylmethyl)- l -cysteine was synthesized from l -serine and 2-ethylhexylthioglycolate using intact cells of recombinant E. coli with high tryptophan synthase activity, and subsequently hydrolyzed to l -CMC with alkali in one reactor. Under optimum conditions established for l -CMC synthesis, 159 g. l −1 of l -CMC was formed at a molar yield of 94% based on when both l -serine and 2-ethylhexylthioglycolate were added. Synthesized l -CMC was confirmed to be l -form after isolation and identification of the product. |
| Databáze: | OpenAIRE |
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