Resolution and synthesis of optically active alcohols with immobilized ovalbumin and pea protein as new bio-catalysts.
It was found that ovalbumin stereoselectively oxidized one of the enantiomers of p-substituted racemic alcohols, thereby providing optically active alcohols with high optical purities. It was found out that, when used appropriately in combination with immobilized pea protein, immobilized ovalbumin made it possible to resolve and synthesize racemic 1-(2-naphthyl)ethanol, 1-phenylethanol, and 1-phenyl-1-propanol. Immobilized ovalbumin could be continuously recycled at least three times without lowering the yield and purity of the products. These results suggested that cereals, beans, and ovalbumin might have additional fourth function among conventional foods. Namely, there might contain nutritional, sensory, biologically regulatory and bio-catalytic functions in conventional foods.
Nagaoka
H
H
Sanyo Shokuhin Co., Ltd., Maebashi Gunma, Japan. hnagaoka@sanyofoods.co.jp
Kayahara
H
H
Wakabayashi
Y
Y
D000438:Alcohols / Q000378:metabolism*; D000818:Animals; D002645:Chickens; D010047:Ovalbumin / Q000378:metabolism*; D010084:Oxidation-Reduction; D018532:Pisum sativum; D010940:Plant Proteins / Q000378:metabolism*
D000438:Alcohols; D010940:Plant Proteins; D010047:Ovalbumin