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Purification and characterization of hydroperoxide lyase from amaranth tricolor (Amaranthus mangostanus L.) leaves

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Abstract

Hydroperoxide lyase (HPL) was extracted from amaranth tricolor leaves using Triton X-100, and purified to electrophoretic homogeneity by ammonium sulfate precipitation, ion-exchange chromatography, hydrophobic interaction chromatography and hydroxyapatite chromatography. The purified HPL preparation consisted of a single band and spot with a molecular mass of about 55 kDa as shown in SDS–PAGE and 2-D PAGE, respectively; the isoelectric point was found to be about 5.4. The maximum activity of the enzyme was observed at pH 6.0 and 25 °C, respectively. The HPL showed higher activity against 13-hydroperoxy-linolenic acid compared to 13-hydroperoxy-linoleic acid. K m value for 13-hydroperoxy-linolenic acid was 62.7 μM, and the corresponding V max was 178.5 μM min−1. The activity of HPL was significantly inhibited by nordihydroguaiaretic acid, HgCl2 and 2(E)-hexenal but not by EDTA and hexanal.

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Acknowledgments

We gratefully acknowledge the financial support received from National 863 Plans Project Foundation of P.R. China (2008AA10Z305 and 2008AA10Z312), National Natural Science Foundation of P.R. China (20876069) and Novozyme Research & Development Centre of P.R. China. The authors are also thankful for the support by the Fundamental Research Funds for the Central Universities (JUSRP10919).

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Authors and Affiliations

  1. State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, Jiangsu Province, People’s Republic of China

    Zhen Long, Xiangzhen Kong, Caimeng Zhang, Bo Jiang & Yufei Hua

  2. School of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, Jiangsu Province, People’s Republic of China

    Zhen Long, Xiangzhen Kong, Caimeng Zhang, Bo Jiang & Yufei Hua

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  1. Zhen Long
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  2. Xiangzhen Kong
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Correspondence to Yufei Hua.

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Long, Z., Kong, X., Zhang, C. et al. Purification and characterization of hydroperoxide lyase from amaranth tricolor (Amaranthus mangostanus L.) leaves. Eur Food Res Technol 231, 865–871 (2010). https://doi.org/10.1007/s00217-010-1337-0

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  • DOI: https://doi.org/10.1007/s00217-010-1337-0

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