Two pectic lyases, L 1 and L 2 , from culture liquids of Aureobasidium pullulans LV 10 were partially purified by ultrafiltration, CM‐Sepharose 6B, DEAE‐cellulose and/or Sephadex G 100 column chromatography, and characterized. L 1 and L 2 showed optimum activity at pH 5 and 7.5 respectively, and at 40°C. The molecular weights of the enzymes determined by gel filtration were estimated to be 89000 1000 and 55000 1000 for L 1 and L 2 respectively. Both lyases were activated by Ca 2+ ions. L 1 attacked highly esterified pectins, L 2 attacked low methoxy‐pectins in preference to polygalacturonic acid.
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Parini et al. (1988) studied this question.
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