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Characterization and functional properties of lactosyl caseinomacropeptide conjugates

AuthorsMoreno, F. Javier ; López-Fandiño, Rosina ; Olano, Agustín
KeywordsLactosylated forms
Functional properties
Maillard reaction
Issue Date2002
PublisherAmerican Chemical Society
CitationJournal of Agricultural and Food Chemistry 50(18): 5179-5184 (2002)
AbstractOvine caseinomacropeptide (CMP) was modified with lactose through Maillard reaction under 44% relative humidity and 40°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 NH2-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.
Identifiersdoi: 10.1021/jf020118u
issn: 0021-8561
e-issn: 1520-5118
Appears in Collections:(IFI) Artículos
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