Heat-induced changes in casein-derived phosphopeptides.
Phosphopeptides derived from casein may function as carriers for calcium and trace elements. In regard to such specific nutritive effects, the heat-induced changes in tryptic phosphopeptides liberated from bovine sodium caseinate as a model system were investigated. Both microwave and oven heating resulted in a marked loss of peptide-bound phosphorous (dephosphorylation) and a decrease of casein-phosphopeptides in the soluble part of the tryptic hydrolysate. It is concluded that hydrolysis of phosphoseryl to seryl residues was the prevailing degradation step to soluble proteolytic products, whereas lysinoalanyl-casein is claimed to be present almost exclusively in the pH 4.6-insoluble part of the tryptic digest.
Meisel
H
H
Institute for Chemistry and Physics, Federal Dairy Research Centre, Kiel, FRG.
Andersson
H B
HB
Buhl
K
K
Erbersdobler
H F
HF
Schlimme
E
E
D000818:Animals; D002364:Caseins / Q000737:chemistry* / Q000528:radiation effects; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008872:Microwaves; D010748:Phosphopeptides / Q000378:metabolism* / Q000528:radiation effects
D002364:Caseins; D010748:Phosphopeptides