Characterization of peroxidase in buckwheat seed.
作者： Tatsuro Suzuki , Yutaka Honda , Yuji Mukasa , Sun-ju Kim
DOI: 10.1016/J.PHYTOCHEM.2005.11.014
关键词:
摘要: A peroxidase (POX)-containing fraction was purified from buckwheat seed. The POX consisted of two isozymes, I and II, that were 6.6- 67.4-fold, respectively. Their molecular weights estimated to be 46.1 kDa (POX I) 58.1 II) by gel filtration. While II each oxidized quercetin, o-dianisidine, ascorbic acid guaiacol, only ABTS. Kinetic studies revealed had lower K(m) values for quercetin (0.071 0.028 mM), ABTS (0.016 mM (0.043 0.029 mM) than o-dianisidine (0.229 0.137 guaiacol (0.288 0 ). optimum pHs various substrates almost the same, except quercetin; pH 8.0 4.5 II. optimal temperatures 30 degrees C 10 II), more stable above C.
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