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• W2054435542 abstract "Abstract To examine residual lipase activities in UHT-processed milk samples, two protein isolates were prepared, one from aqueous supernatant and the other from milk fat globule membrane. Results of DEAE-cellulose chromatography indicated that the protein isolates from the aqueous supernatants contained three lipase-active fractions; the proteins from the milk fat globule membranes exhibited only one lipase-active fraction. Analysis by SDS-PAGE revealed that the lipase-active fractions from the aqueous supernatants contained a major or minor κ-casein component, as well as other caseins and whey proteins. However, the lipase-active fraction from the milk fat globule membranes was composed mainly of α-casein. When a pool of the lipase-active fractions from the aqueous supernatants was incubated with a milk fat emulsion at 35°C for 4 h, the fractions hydrolyzed butyric acid the most, followed by caproic and palmitic acids. However, the lipase-active fraction from the milk fat globule membranes hydrolyzed palmitic and stearic acids most, followed by linoleic and oleic acids." @default.
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• W2054435542 date "1994-08-01" @default.
• W2054435542 modified "2023-09-28" @default.
• W2054435542 title "Isolation of Lipase-Active Fractions from Ultra-High Temperature-Processed Milk and Their Patterns of Releasing Fatty Acids from Milk Fat Emulsion" @default.
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• W2054435542 doi "https://doi.org/10.3168/jds.s0022-0302(94)77159-9" @default.
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