Overphosphorylation of milk caseins by a recombinant protein kinase CK2 catalytic subunit
1999
Milk caseins have been phosphorylated by a recombinant protein kinase CK2 catalytic subunit from Schizosaccharomyces pombe (rspCK2alpha). Phosphate incorporation stoechiometries into purified caseins and into native phosphocaseinate, a substrate exhibiting a micellar-like structure, were determined. We incorporated 2.01 mol of P/mol of alpha-casein, 6.46 mol of P/mol of alpha-casein, up to 0.29 mol of P/mol of kappa-casein in 4 h, and more than 1.36 mol of P/mol of casein into phosphocaseinate under optimized conditions. Phosphocaseinate was sequentially phosphorylated; beta-caseins being labeled at first; alpha-caseins being labeled later; and to a lower extend, kappa-caseins were the last to be phosphorylated. The solubility of phosphocaseinate micelles increased by 1.34 from 65 to 87%, and its rennetting time was increased 2.88 times. These results are discussed in terms of plausible structural organization of caseins micelles and the effect of phosphorylation on their structure.
اظهر المزيد [+] اقل [-]الكلمات المفتاحية الخاصة بالمكنز الزراعي (أجروفوك)
المعلومات البيبليوغرافية
تم تزويد هذا السجل من قبل National Agricultural Library
