Enzymatic Resolution of Racemic Amino Acids
| Autor: | Harumi Tsuda, Kimiyo Michi |
|---|---|
| Rok vydání: | 1955 |
| Předmět: |
Ammonium sulfate
Resolution (mass spectrometry) Stereochemistry chemistry.chemical_element Fractionation Calcium medicine.disease_cause Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry Hydrolysis chemistry.chemical_compound Adsorption Mold medicine Acetone Organic chemistry Molecular Biology chemistry.chemical_classification Chromatography Elution Organic Chemistry General Medicine Amino acid Enzyme chemistry Biotechnology |
| Zdroj: | Bulletin of the Agricultural Chemical Society of Japan. 19:153-158 |
| ISSN: | 1881-1272 0375-8397 |
| DOI: | 10.1271/bbb1924.19.153 |
| Popis: | In this paper further purification procedures for the preparation of mold acylase and the enzymatic susceptibility of acylated amino acids are described, together with the resolution of DL-phenylalanine and DL-methionine.The mold acylase of P. vinaceous was prepared by fractionation with 0.6 saturation of ammonium sulfate, acetone precipitation, calcium gel adsorption and following elution with phosphate buffer. The enzyme was more effective toward the acylderivatives of aromatic substituted amino acids than toward those of the aliphatic amino acids and it had little or no action upon acylated D-amino acids. By utilizing the optical specificity of the enzyme, DL-phenylalanine and DL-methionine were resolved to the optical enantiomorphs. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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