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Conference abstract, 2006

Activities of phospholipid acyl hydrolase, wax ester synthetase and ethanol esters synthase differ between young and mature parts of wheat roots and are strongly activated by grass herbicides

Banas, Walentyna; Olsson, Peter; Banas, Antoni; Stymne, Sten

Abstract

Recently we have shown that microsomal membranes from Arabidopsis leaves and roots as well as wheat roots can efficiently acylate free fatty acids (without prior activation to acyl-thioesters) to long chain alcohols. These membranes also acylate free fatty acid to ethanol in producing ethanol esters. Production of ethanol esters positively correlated with phospoholipase activity in assays with wheat root extracts. In the presented study we show, using both microsomal preparation and crude extract of wheat roots, that phospholipid acyl hydrolase activity is several times higher in older part of roots compared with root tips which contains meristematic and elongating cells. When the wheat roots were grown in the presence of alloxydim (a grass herbicide) for a 48hrs, the phospholipid acyl hydrolase activity increased about 20 times in root tips but only about 2 times in older part of roots. The phospholipid acyl hydrolase activity positively correlated with utilisation of free fatty acids for ethanol ester and wax ester synthesis. The two latter activities were several times higher in older parts of wheat roots compared to root tips but were greatly stimulated in root tips by alloxydim treatment. All three enzymatic activities observed in wheat roots were very efficiently inhibited by low concentrations of tetrahydrolipstatin, an inhibitor of certain lipases, suggesting that the enzymes share a common lipase mode of action

Published in

Conference

17th International Symposium on Plant Lipids

Authors' information

Swedish University of Agricultural Sciences, Department of Crop Science
Banas, Antoni
Olsson, Peter
Banas, Walentyna

UKÄ Subject classification

Agricultural Science
Food Science

URI (permanent link to this page)

https://res.slu.se/id/publ/11148