Enzymatic phosphorylation of food proteins by purified and recombinant protein kinase CK2
1998
Chardot, T. | Benetti, P.H. | Canonge, M. | Kim, S.-I. | Chaillot, D. | Fouques, D. | Meunier, J.-C.
The autors studied some functional properties of phjosphorylated caseins. Solubility was improved for all pH values but pI. Sensitivity to calcium has also been assessed, and it is slightly improved upon phosphorylation. They havecloned the catalytic subunit of protein kinase CK2 from yeast Y. lipolytica. The recombination catalytic subunit expressed in E. coli was active and displayed kinetic properties similar to those of the purified enzyme. The recombinant catalytic subunit was able to phosphorylate plant reserve proteins and milk proteins to a significant extent. Best substrates were soy ss-conglycinin (1.0 P/mol), and glycinin (0.59 P/mol).
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