Model studies on reactions of plant phenols with whey proteins.
Whey proteins were modified by reaction with selected phenolic compounds (ferulic-, chlorogenic-, caffeic- and gallic acid) and related substances (quinic acid and p-quinone) as well as with extracts from coffee, tea, potato and pear at pH 9. The derivatives formed were characterized in terms of their physicochemical and digestion properties. The derivatization was accompanied by a reaction at the lysine and tryptophan side chains, whereby their content was decreased in comparison to that in the control whey proteins. Moreover, the solubility of the derivatives decreased over a broad pH range and the derivatization influenced the hydrophobe-hydrophile character of the whey proteins. The isoelectric points were shifted to lower pH values in the order of reactivity as follows: gallic acid > p-quinone > caffeic acid > chlorogenic acid. The other derivatives showed no or few changes compared to the control whey proteins. The formation of high molecular fractions was documented with SDS-PAGE. Especially the derivatives of chlorogenic-, caffeic-, gallic acid and p-quinone showed an increase in molecular weight of beta-lactoglobulin fraction from 18,300 to 20,000 Da. A dimer formation in molecular range 40,000 was also registered. MALDI-TOF-MS was applied to characterize the binding of the individual phenolic compounds or their oxidation products to the whey protein fractions, alpha-lactalbumin and beta-lactoglobulin. In vitro experiments showed that the digestion of the derivatized whey proteins with the enzymes of the gastrointestinal tract (trypsin, chymotrypsin, pepsin and pancreatin) was adversely effected. Similar results with regard to physicochemical characterization and digestion properties of the whey proteins treated with the applied extracts from plant beverages, fruit and vegetable were also documented. Coffee and tee were comparatively the most reactive extracts.
Rawel
H M
HM
University of Potsdam, Institute of Nutritional Science, Arthur-Scheunert-Allee 114-116, D-14558 Bergholz-Rehbrücke, Germany.
Kroll
J
J
Hohl
U C
UC
D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007526:Isoelectric Point; D013058:Mass Spectrometry; D008894:Milk Proteins / Q000737:chemistry*; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010636:Phenols / Q000737:chemistry*; D010936:Plant Extracts / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry; D012995:Solubility; D013499:Surface Properties; D014364:Tryptophan / Q000737:chemistry; D000067816:Whey Proteins
D008894:Milk Proteins; D010636:Phenols; D010936:Plant Extracts; D010940:Plant Proteins; D000067816:Whey Proteins; D014364:Tryptophan