Journal
EUROPEAN FOOD RESEARCH AND TECHNOLOGY
Volume 234, Issue 4, Pages 723-731Publisher
SPRINGER
DOI: 10.1007/s00217-012-1685-z
Keywords
Hydroperoxide lyase; Solanum tuberosum; Characterization; 13-Hydroperoxy-linolenic acid; 13-Hydroperoxy-linoleic acid
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Funding
- 973 Project [2012CB720802]
- Natural Science Foundation of China [31171705, 20906040]
- 863 Project [2011AA100904]
- Support Project of Jiangsu Province [BE2011622, BE2011766, BE2010678, BE2010626]
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A cDNA encoding hydroperoxide lyase (HPL) was isolated from Solanum tuberosum, cloned into pQE-30 vector, and expressed in E. coli. The recombinant protein was purified by nickel affinity chromatography and showed an approximate molecular weight of 54 kDa by SDS-PAGE analysis, which was similar to the predicted value based on the putative amino acid sequences (53.9 kDa). 13-Hydroperoxy-linolenic acid (13-HPOT) was the preferred substrate for the enzyme compared with 13-hydroperoxy-linoleic acid (13-HPOD). The corresponding volatile products were 2(E)-hexenal and n-hexanal tested by headspace-gas chromatography, respectively. The enzyme was optimally active at 25 A degrees C and pH 6.5. The K (m), V (max), and the catalytic efficiency (V (max)/K (m)) for 13-HPOT were 56.6 mu M, 71.3 units/mg, and 1.26 units/mg center dot mu M, respectively. Activity of the recombinant potato HPL increased when Triton X-100, sodium chloride, or potassium chloride was added in the reaction mixture, while calcium chloride decreased activity of the recombinant enzyme.
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