Abstract
The effects of pH, ionic strength, temperature, and degree of polymerization of procyanidins isolated from Rhaphiolepis umbellata on the formation of procyanidin-protein complexes were investigated. The results suggested that the formation of the complexes was strongly influenced by pH, and no insoluble complex was detected above pH 10.5, that the affinity of procyanidins for proteins was proportional to the degree of polymerization of procyanidins, and dimers and higher oligomers of procyanidins could form insoluble complexes with proteins, and that the structural isomers of dimers or trimers of procyanidins also had higher affinities for proteins, forming insoluble complexes.
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