Document Detail


Resolution and synthesis of optically active alcohols with immobilized ovalbumin and pea protein as new bio-catalysts.
MedLine Citation:
PMID:  11330679     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
H Nagaoka; H Kayahara; Y Wakabayashi
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  65     ISSN:  0916-8451     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2001 Mar 
Date Detail:
Created Date:  2001-05-01     Completed Date:  2001-10-25     Revised Date:  2003-11-14    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  634-7     Citation Subset:  IM    
Affiliation:
Sanyo Shokuhin Co., Ltd., Maebashi Gunma, Japan. hnagaoka@sanyofoods.co.jp
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MeSH Terms
Descriptor/Qualifier:
Alcohols / metabolism*
Animals
Chickens
Ovalbumin / metabolism*
Oxidation-Reduction
Peas
Plant Proteins / metabolism*
Chemical
Reg. No./Substance:
0/Alcohols; 0/Plant Proteins; 9006-59-1/Ovalbumin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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