Abstract
Polygalacturonic acid trans-eliminase (PATE) was purified from the culture fluid of Erwinia carolovora, completely free from contamination by polygalacturonase and pectinesterase. The enzyme attacks polygalacturonic acid, in preference to pectin; however, pectin is attacked to an extent dependent upon the degree of demethoxylation of the pectin molecule. Polygalacturonic acid and oligouronides are degraded by Erwinia PATE at rates which decrease as the chain length of the substrate decreases; digalacturonic and unsaturated digalacturonic acids are not attacked by this enzyme. Erwinia PATE acts randomly, has an optimum pH of 8.5, and is stimulated by calcium. The major endproduct from polygalacturonic acid is O-(4-deoxy-β- l-5- threo-hexopyranos-4-enyluronic acid)-(1→4)- d-galacturonic acid (“unsaturated digalacturonic acid”); lesser amounts of unsaturated trigalacturonic acid and saturated mono- and digalacturonic acids are formed. From the cells of the same organism, an intracellular enzyme wag isolated which has properties similar to those of the extra-cellular polygalacturonic acid trans-eliminase.
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