期刊
EUROPEAN FOOD RESEARCH AND TECHNOLOGY
卷 231, 期 6, 页码 865-871出版社
SPRINGER
DOI: 10.1007/s00217-010-1337-0
关键词
Amaranth tricolor; C6 aldehydes; Hydroperoxide lyase; Purification
资金
- National 863 Plans Project Foundation of P.R. China [2008AA10Z305, 2008AA10Z312]
- National Natural Science Foundation of P.R. China [20876069]
- Novozyme Research & Development Centre of P.R. China
- Fundamental Research Funds for the Central Universities [JUSRP10919]
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 A degrees 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 mu M, and the corresponding V (max) was 178.5 mu M min(-1). The activity of HPL was significantly inhibited by nordihydroguaiaretic acid, HgCl(2) and 2(E)-hexenal but not by EDTA and hexanal.
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