Resolution and synthesis of optically active alcohols with immobilized ovalbumin and pea protein as new bio-catalysts.

Article abstract of DOI:10.1271/bbb.65.634

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.

Full text of DOI:10.1271/bbb.65.634

Bioscience, Biotechnology, and Biochemistry
ISSN: 0916-8451 (Print) 1347-6947 (Online) Journal homepage: http://www.tandfonline.com/loi/tbbb20
Resolution and Synthesis of Optically Active
Alcohols with Immobilized Ovalbumin and Pea
Protein as New Bio-catalysts
Hiroyuki NAGAOKA, Hiroshi KAYAHARA & Yasushi WAKABAYASHI
To cite this article: Hiroyuki NAGAOKA, Hiroshi KAYAHARA & Yasushi WAKABAYASHI (2001)
Resolution and Synthesis of Optically Active Alcohols with Immobilized Ovalbumin and Pea
Protein as New Bio-catalysts, Bioscience, Biotechnology, and Biochemistry, 65:3, 634-637, DOI:
10.1271/bbb.65.634
To link to this article: http://dx.doi.org/10.1271/bbb.65.634
Published online: 22 May 2014.
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Date: 05 November 2015, At: 19:06