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- W2040607367 abstract "In a previous paper (2) results were presented on studies of tipolysis in homogenized milk and cream, which indicated that lipase activity in homogenized milk was not always affected to the same extent, if at all, by those factors which influence the enzymic action in unprocessed raw milk. The results presented herein constitute a continuation of these studies. The influence of pH on lipase action in homogenized milk has been studied only to a limited extent although Dorner and Widmer (1) observed that acidifying homogenized raw milk with tIC1 retarded or even completely prevented rancidity development. However, in studies on non-homogenized milk, Mattick and Kay (4) found fat hydrolysis to be greatest at pH 8.2-8.7 and Roahen and Sommer (7) secured a somewhat similar optimum range of pH 8.4--8.6. The non:specificity of milk lipase has been indicated by many workers in that certain specific fat acid esters have been utilized as the substrate for lipase action. Rogers, Berg and Davis (8) early used ethyl butyrate as a base for lipase action and more recently Mattick and Kay developed a method for measuring activity of the fat splitting enzyme in milk by its ability to hydrolyze tributyrin. Tarassuk and Palmer (9) indicate that milk lipase will hydrolyze the esters of lauric, myristic and palmitic acids. Later, Palmer and Hankinson (6) dispersed diglycol laurate, diglycol oleate, ethyl myristate and butyl stearate in raw skim milk by shaking, and secured hydrolysis in every case. Hydrolysis of butterfat may be produced by enzymes from other sources than milk. Palmer (5) used a glycerine extract of pigs pancreas and later commercial steapsin to produce lipolysis. Tarassuk and Richardson (10) produced lipolysis in pasteurized cream with steapsin." @default.
- W2040607367 created "2016-06-24" @default.
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- W2040607367 date "1942-10-01" @default.
- W2040607367 modified "2023-09-26" @default.
- W2040607367 title "Influence of pH, Type of Fat, and Pancreatic Extract upon Lipolysis in Homogenized Milk" @default.
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- W2040607367 doi "https://doi.org/10.3168/jds.s0022-0302(42)95349-9" @default.
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