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'Fatty Acid Hydroperoxide' in keywords
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1992 (1)
1982 (1)
1Author    P. Schreier, G. LorenzRequires cookie*
 Title    Separation, Partial Purification and Characterization of a Fatty Acid Hydroperoxide Cleaving Enzyme from Apple and Tomato Fruits  
 Abstract    A membrane-bound enzyme catalysing the cleavage o f 13-hydroperoxy-(Z)-9,(£)-l 1-oc-tadecadienoic acid (13-LHPO) and 13-hydroperoxy-(Z)-9,(£)-ll,(Z)-15-octadecadienoic acid (13-LnHPO) to C6-aldehydes was isolated and partially purified from apples and tomatoes. At­ tempts to employ Ultrogel AcA 34 and AcA 22 in a gel chromatographic purification step were partially frustrated by reaggregation phenomena. However, by using Sepharose CL-4 B an en­ zyme fraction (MW 200 000 Da) with lipoxygenase and fatty acid hydroperoxide cleaving activity could be separated from a high molecular-weight active eluate. By applying preparative isoelec­ tric focussing to the tomato protein we succeeded in separating the fatty acid cleaving activity from the lipoxygenase, because o f their different isoelectric points of pH 5.8 -6 .1 and pH 5.0, re­ spectively, An 8.4-fold purification o f the fatty acid cleaving activity was achieved. A pH-op-timum of 5.5 and a K m-value o f 2.6 x 10~5 m/1 for the 13-hydroperoxide o f linoleic acid were mea­ sured. p-Chloromercuribenzoic acid (1 mM) showed significant inhibitory effect on the fatty acid hydroperoxide cleaving enzyme, but no evidence o f inhibition was found with 1 mM H20 2, KCN, DABCO and EDTA or superoxide dismutase (270 U). The maximum amount of fatty acid hydroperoxide decomposition (C8-aldehyde formation) was determined to be 59%. 
  Reference    Z. Naturforsch. 37c, 165—173 (1982); received August 18/N ovem ber 24 1981 
  Published    1982 
  Keywords    Apples, Tomatoes, Fatty Acid Hydroperoxides, Cleavage Enzyme, Cg-Aldehydes 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0165.pdf 
 Identifier    ZNC-1982-37c-0165 
 Volume    37 
2Author    AkikazuH. Atanaka, T. Adahiko Kajiwara, Kenji Matsui, Hiromitsu ToyotaRequires cookie*
 Title    Substrate Specificity of Tea Leaf Hydroperoxide Lyase  
 Abstract    Substrate specificity o f tea leaf fatty acid hydroperoxide lyase was systematically investigat­ ed using an entire series o f co6-(5)-hydroperoxy-C14-C24 dienoic and trienoic acids as sub­ strates. Unexpectedly, the hydroperoxides o f C22 but not natural substrates, i.e., those o f C 18, showed the highest reactivities for the lyase. The reactivities o f the hydroperoxides o f trienoic acids were always four to ten times higher than those o f the dienoic acids. 
  Reference    Z. Naturforsch. 47c, 677—6 (1992); received June 24/July 24 1992 
  Published    1992 
  Keywords    Aldehyde, Fatty Acid Hydroperoxide, Hydroperoxide Lyase, Substrate Specificity, Tea Leaf 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0677.pdf 
 Identifier    ZNC-1992-47c-0677 
 Volume    47