Enzymatic Maceration Mechanism in Biochemical Pulping of Mitsumata (Edgeworthia papyriferaSieb. et Zucc) Bast

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Abstract
In a comparison of the crude enzyme secreted by the bacterium Erwinia carotovora FERM P-7576 with the corresponding purified overall endo-pectate lyase (endo-PATE) pI (isoelectric point)-isozymes on a basis of equal activity and constitution, the former was found to have higher maceration activity for biochemical pulping of caustic soda-presoaked mitsumata (Edgeworthia papyrifera Sieb. et Zucc) bast than the latter. These results indicate that some additional enzyme (s) other than endo-PATE are required for the maceration. Focusing on the maceration activity, the intensive purification of the crude enzyme was conducted and another maceration factor was successfully isolated, which was identified as endo-pectin lyase (endo-PNTE). The isolated endo-PNTE was found to have a molecular weight of 39,000, pI of 8.2 and a specific activity of 7,911 units/mg. The enzymatic maceration of this bast fiber was concluded to be due only to a concerted action of these two enzymes.