![Sample our Physical Sciences journals, sign in here to start your FREE access for 14 days]({"type":"image" , "src" : "/sda/110819/TOC-Subject-Sample-2021-Physical-Sciences.jpg"})
Abstract
The effects of enzymatic phosphorylation on the functional properties of soybean proteins were investigated. As previously reported, among soybean proteins, 11S acidic subunits (AS) have been phosphorylated by cyclic adenosine monophosphate-dependent protein kinase (A-kinase). Upon the phosphorylation (2 mol/mol 11S AS), the Ca2+-sensitivity of 11S AS decreased and the emulsion properties were improved. On the other hand, the foaming properties and pH-solubility were not so affected. In the interaction with Ca2+, 11S AS were found to become resistant to Ca2+ upon phosphorylation, as shown by UV spectra. Further relationships between the functionality and protein conformation are discussed.