Food and Fermentation Industries >

2011 , Vol. 37 >Issue 02: 17 - 20

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.2011.02.030

Food and Fermentation Industries

Screen and Purification of Hydroperoxide Lyase

  • Long Zhen ,
  • Ruan Qi-Jun ,
  • Kong Xiang-zhen ,
  • Zhang Cai-meng ,
  • Hua Yu-fei ,
  • Jiang Bo
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Online published: 2011-02-25

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Abstract

Amaranthus tricolor leaves were identified as a particularly rich source of HPL activity.Hydroperoxide lyase(HPL) was purified to electrophoretic homogeneity from high speed centrifigation,solubilized by Tritron X-100,ammonium sulfate precipitation,hydroxypatite chromatography and DEAE Toyopearl chromatography.The purified HPL preparation consisted of a single band with a molecular mass of about 55 ku in SDSPAGE.The HPL showed higher activity against 13-hydroperoxy-linolenic acid compared to 13-hydroxy-linoleic acid.Maximum HPL activity was observed at pH 6.0 and 25℃,and room temperature sustains high enzyme activity.

Key words： hydroperoxide lyase; amaranth tricolor; purification; characteristics

Cite this article

Long Zhen , Ruan Qi-Jun , Kong Xiang-zhen , Zhang Cai-meng , Hua Yu-fei , Jiang Bo . Screen and Purification of Hydroperoxide Lyase[J]. Food and Fermentation Industries, 2011 , 37(02) : 17 -20 . DOI: 10.13995/j.cnki.11-1802/ts.2011.02.030

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