Characterization and functional properties of lactosyl caseinomacropeptide conjugates.
Ovine caseinomacropeptide (CMP) was modified with lactose through Maillard reaction under 44% relative humidity and 40 degrees C for various periods (0-11 days). Different lactosylated CMP forms were separated by capillary electrophoresis and reversed phase high-performance liquid chromatography (RP-HPLC) and identified by RP-HPLC coupled with electrospray ionization mass spectrometry (ESI-MS). Around 55-60% of CMP was lactosylated under the conditions assayed, with the monolactosylated form being the most abundant one, followed by the di-, tri-, and tetralactosylated species. During the first days of incubation amino acid analyses showed a decrease in lysine and NH(2)-terminal methionine, which coincided with an increase in the furosine content. However, from the ninth day of incubation, further degradation of Amadori compounds prevailed over their formation. Solubility, heat stability, and emulsifying capacity of the native and modified CMP were investigated. Lactosylation improved the emulsifying activity, but it did not modify the great solubility and heat stability of native CMP.
Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva 3, 28006 Madrid, Spain.
F Javier
FJ
Moreno
Rosina
R
López-Fandiño
Agustín
A
Olano
D000818:Animals; D002364:Caseins / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D004355:Drug Stability; D019075:Electrophoresis, Capillary; D005260:Female; D006358:Hot Temperature; D007785:Lactose / Q000737:chemistry*; D008239:Lysine / Q000032:analysis; D015416:Maillard Reaction; D008715:Methionine / Q000032:analysis; D008892:Milk / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D012756:Sheep; D012995:Solubility; D021241:Spectrometry, Mass, Electrospray Ionization
D002364:Caseins; D010446:Peptide Fragments; C065989:caseinomacropeptide; D008715:Methionine; D007785:Lactose; D008239:Lysine