Abstract
The berry protein composition of 28 muscadine cultivars was studied using a combination of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and capillary electrophoresis. A wide variation in berry protein content and composition was observed. Total berry protein content ranged from 1.6 to 5.6%. SDS-PAGE resolved the berry proteins into 13 distinct polypeptides, ranging in molecular weights from 10 to 100 kDa. One of the doublet bands of 30 kDa was found to be cultivar specific, being present in certain cultivars and absent in Welder, Sweet J, Dixie, and Jane Bell. Capillary electrophoresis resolved both the buffer-soluble (pH 8.3) and acid-soluble (pH 3.5) berry proteins into >20 components. The cultivar Rosa exhibited the maximum number (24) of buffer-soluble proteins. The acid-soluble proteins of Senoia resolved into fewer components compared to the other samples tested. The results indicated that the berry proteins may be useful as biochemical markers to identify genetic variation in muscadine cultivars.
- Muscadine grapes
- protein
- sodium dodecyl sulfate-polyacrylamide gel electrophoresis
- capillary electrophoresis
- Copyright 2002 by the American Society for Enology and Viticulture
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