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Polyphenol Oxidase from Bean Sprouts (Glycine
max l.)
January/ February 2003
Journal of Food Science Vol. 68, No. 1, 2003
T. Nagai and N. Suzuki
Abstract:
Polyphenol oxidase (PPO) was purified and characterized from bean sprouts by
ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Toyopearl 650M,SuperQ-Toyopearl 650S and QAE-Toyopearl 550C column chromatographies.
Substrate staining of the crude extract on electrophoresis showed the
presence of 2 isozymic forms of this enzyme. The molecular weight of the
purified enzyme was estimated to be about 54 kDa. The optimum pH was 9.0 and
optimum temperature 40 8C. Heat inactivation occurred about 30 8C. PPOshowed activity to catechol, pyrogallol and dopamine. These compounds such
as ascorbic acid, L-cysteine, 2-mercaptoethanol, and glutathione used was
the effective inhibitor. Enzyme activity was maintained for 7 d at 4 8C but
suddenly decreased after 8 d.
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