Purification and characterization of hydroperoxide lyase from amaranth tricolor (Amaranthus mangostanus L.) leaves |
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| Authors: | Zhen Long Xiangzhen Kong Caimeng Zhang Bo Jiang Yufei Hua |
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| Affiliation: | (1) State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, Jiangsu Province, People’s Republic of China;(2) School of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, Jiangsu Province, People’s Republic of China; |
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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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