Maceration of Plant Tissues by Pectin trans-Eliminase

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Eliminative Cleavage of Pectin and of Oligogalacturonide Methyl Esters by Pectin Trans-eliminase.

In the preceding paper (1) a method was described for the purification of the extracellular pectin trans-eliminase of Aspergillus jonsecaeus. The enzyme was purified by a three-step procedure to the point at which other pectic enzymes and cellulase were no longer detectable. The effects of pH, of Na+, Mg++, and Ca++ ions, and of a few anions on the activity of the enzyme were also reported. In ...

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Purification and Certain Properties of Pectin Trans-eliminase from Aspergillus Fonsecaeus.

In 1960 Albersheim, Neukom, and Deuel (1) reported on an enzyme present in a commercial pectic enzyme preparation (Pectin01 RlO, Rohm and Haas Company, Philadelphia) that degraded the a, 1 + 4-glycokidic bonds in pectin by a trans elimination of the proton on the 5th carbon atom of an anhydromethyl galacturonate unit with the oxygen of the adjacent glycosidic bond. Cleavage of the bonds in pect...

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Pectin methylesterase, metal ions and plant cell-wall extension. Hydrolysis of pectin by plant cell-wall pectin methylesterase.

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Analysis of the Components Released from Potato Tuber Tissues during Maceration by Pectolytic Enzymes.

Endo-pectin lyase and endo-polygalacturonase of Aspergillus japonicus attack the middle lamella of plant tissue and cause tissue maceration. Galacturonides, neutral sugars, and proteins were released from potato tuber tissues during maceration by both purified enzymes. These three components accounted for 92% of the soluble products. The neutral sugars released were rhamnose, arabinose, and gal...

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Oxidation of paraffins by plant tissues.

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ژورنال

عنوان ژورنال: Agricultural and Biological Chemistry

سال: 1971

ISSN: 0002-1369,1881-1280

DOI: 10.1271/bbb1961.35.1157