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Plant and Cell Physiology, 1990, Vol. 31, No. 2 233-240
© 1990

Article

Betacyanin-Decolorizing Enzymes from Phytolacca americana

Keiro Kumon, Jiro Sasaki, Mototaro Sejima, Yasuyoshi Takeuchi and Yoshiyuki Hayashi

Aburahi Laboratories, Shionogi Research Laboratories, Shionogi and Co., Ltd. Gotanda, Koka-cho, Koka-gun, Shiga-ken, 520-34 Japan

Betacyanin-decolorizing enzymes (BDEs) in Phytolacca americana were partially purified and characterized. Acidic enzymes, BDE1 and BDE2, and basic enzymes, BDE3 and BDE4, were partially purified by column chromatography on DEAE-Sepharose CL-6B and CM-Sepharose CL-6B. These enzymes degraded betanin to its aglycon (betanidin) and then to a product with a peak of absorbance at 485 nm. The optimum pH values were 5.0 for BDE1, 3.5 for BDE2, and 5.5 for BDE3 and BDE4. BDE activity was detected in extracts of the leaf, stem, seed, and root. The highest specific activity of BDE2 was found in the red epidermis of the stem. The activity of BDE2 was inhibited by NH4NO3, KNO3, KC1, and NaCl, but the activities of the other BDEs were not inhibited. These results suggest that BDEs other than BDE2 control the degradation of betacyanin in the intracellular space.

(Received March 27, 1989; Accepted December 8, 1989)
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