Use of Pectic Enzymes in a Study of the Nature of Intercellular Cement of Tobacco Leaf Cells

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Abstract
A commercial pectinase preparation has been used to separate large quantities of living tobacco leaf cells from each other. An enzyme which is effective in the separation of the cells has been isolated from this preparation. This partially-purified enzyme is 10-15 times as active (protein basis) as the commercial preparation. The enzyme is very effective in hydrolyzing pectic acid, while completely esterified pectic acid is not attacked. It has no proteolytic activity. From the substrate specificity of this enzyme it is suggested that the material binding the leaf cells together is pectic acid with few carboxyl groups esterified. The reaction appears to be complex, however; cell separation involves more than the simple cleaving of pectic acid. On occasion, the enzyme is not very effective in separating cells, but full activity is restored with 0.001 [image] ethylenediaminetetraacetic acid. Ca ion but not Na, K, or Mg interferes in the cell separation reaction at low concentrations. It is suggested that the Ca associated with the middle lamella is rather transitory.

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