Author
 |
SAVARY, BRETT |
|
Submitted to: Meeting Abstract
Publication Type: Other Publication Acceptance Date: 8/14/2002 Publication Date: 8/14/2002 Citation: Savary, B.J. 2002. Purification and propeties of a pectin acetylesterase isolated from tomato fruit. Meeting Abstract in American Society of Plant Biologists, Annual Meeting. Paper No. 303. Interpretive Summary: Technical Abstract: Acetyl esters can occur at C-2 and C-3 hydroxyl groups in galacturonic acid residues of pectin. Some plant materials, such as sugar beet pectin, may contain up to 25% degree of acetylation. These esters can effect major changes in the physical, chemical, and biological properties of pectin. Pectin acetylesterase (EC 3.1.1.6) is capable of specifically hydolyzing such acetyl esters in homogalacturonan regions. This enzyme has been purified previously from citrus peel and mung bean hypocotyl tissues, and it was recently identified as a contaminant enzyme in a commercial tomato fruit-specific pectin methylesterase preparation (Savary, 2001). This presentation will report on the purification of the enzyme from ripe tomato fruit for further biochemical and structural characterization. Details of the chromatographic purification, the electrophoretic properties, and general biochemical features will be provided. This highly pure, well-defined enzyme will be used to explore its biochemical function in the cell wall and for technical modification of pectin structure-functional properties. |
