Resolution and synthesis of optically active alcohols with immobilized water-soluble proteins from green pea, soybean and buckwheat as new bio-catalysts

• Published in: Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2000-04, Vol.64 (4), p.781-784
• Main Authors: Nagaoka, H. (Gifu Univ. (Japan)), Kayahara, H
• Format: Article
• Language: English
• Subjects: (±)-1-(2-naphthyl)ethanol; (±)-1-(4-substituted phenyl)ethanol; ALCOHOLES; ALCOHOLS; Alcohols - chemistry; ALCOOL; BIOCATALIZADOR; BIOCATALYSEUR; BIOCATALYSTS; Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnology; BUCKWHEAT; CHEMICAL SYNTHESIS; Ethanol - analogs & derivatives; Ethanol - chemistry; Fagopyrum - chemistry; Fundamental and applied biological sciences. Psychology; Glycine max - chemistry; GUISANTE; IMMOBILISATION; IMMOBILIZATION; immobilized buckwheat protein; immobilized green pea protein; immobilized soybean protein; INMOVILIZACION; LIGHT; LUMIERE; LUZ; Methods. Procedures. Technologies; Naphthalenes - chemistry; Oxidation-Reduction; PEAS; Pisum sativum - chemistry; Plant Proteins - chemistry; POIS; PROTEINAS; PROTEINE; PROTEINS; SARRASIN; SINTESIS QUIMICA; SOJA; Solubility; SOYBEANS; SYNTHESE CHIMIQUE; TRIGO SARRACENO; Water
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.64.781

Kinetic resolution of racemic alcohols, (+-)-1-(4-substituted phenyl)ethanol and (+-)-1-(2-naphthyl)ethanol, was done with immobilized green pea, soybean, or buckwheat proteins. The resolution was done stereoselectively by oxidizing only one enantiomer of a racemic alcohol to leave an optically active alcohol with a high purity. In addition, each protein could be reused consecutively at least three times without any decrease of yield or optical purity