Effect of dephosphorylation on bovine casein

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DOIResolve DOI: http://doi.org/10.1016/j.foodchem.2006.03.033
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TypeArticle
Journal titleFood Chemistry
Volume101
Issue3
Pages12631271; # of pages: 9
SubjectBovine casein; Dephosphorylation; pha; �-Casein; �-Casein; Acid Phosphatase; phosphatase; Phosphates
AbstractBovine whole casein, a- and �-casein were dephosphorylated by potato acid phosphatase (EC 3.1.3.2); the extents of dephosphorylation were as follows: whole casein 71.6%, a-casein 89.2% and �-casein 73.7%. SDS-PAGE, urea-PAGE, RP-HPLC and ESI-MS demonstrated effects of dephosphorylation on the caseins; a- and �-casein showed both proteolysis and dephosphorylation while whole casein showed only dephosphorylation. Urea-PAGE and ESI-MS confirmed the identities of the individual fractions. ESI-MS established (a) the MW for a- and �-casein as 23 612 and 24 017 kDa, respectively, (b) random removal of 1, 2, 4, 6, 7 and 8 phosphate groups during dephosphorylation of a-casein, (c) random removal of 1, 2, 3, 4 and 5 phosphate groups during dephosphorylation of �-casein and (d) limited dephosphorylation of both a-casein (1 and 2 phosphates) and �-casein (1 phosphate) in the absence of the phosphatase.
Publication date
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number47532
NPARC number3539179
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Record identifier2ff6bf56-8db6-4930-a2b0-283859aa025c
Record created2009-03-01
Record modified2016-05-09
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